DRAMP_ID	Sequence	Hiden_Sequence	Original_Sequence	Sequence_Length	Name	Uniprot_Entry	Family	Source	Activity	Protein_Existence	Secondary_Structure	Structure_Description	PDB_ID	Comments	Target_Organism	Hemolytic_Activity	Linear/Cyclic	N_terminal_Modification	C_terminal_Modification	Special_Amino_Acid_and_Stapling_Position	Stereochemistry	Cytotoxicity	Pubmed_ID	Reference	Author	Title	Specific_Type	Nucleotide_Sequence	Full_Sequence	lfcMLE	padj	Workflow	SMILES
DRAMP21468	KFFⓀKLKⓀAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 2 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 8 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 2 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 16 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 16 μg/mL)	[Ref.32216308] It has 1.9% hemolysis against human red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 4 and 8) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (4) and Ⓚ (8) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C(NC(=O)C1NC(=O)C(CCCC[NH3+])NC(=O)C(CC(C)C)NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc2ccccc2)Cc2ccccc2)CCCC[NH2+]CC=CC[NH2+]CCCC1)C)C(C)C
DRAMP21469	KFFⓀKLKKAVⓀKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 3 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 8 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 8 μg/mL), Listeria monocytogenes (MIC99.9= 8 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 16 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 1.1% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 4 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (4) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC1C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH3+])CCCC[NH3+])Cc2ccccc2)CCCC[NH3+])CCCC[NH2+]CC=CC[NH2+]CCCC1)Cc1ccccc1)Cc1ccccc1)C([NH3+])CCCC[NH3+]
DRAMP21470	KFFKⓀLKKAVKⓀGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 4 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 8 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 8 μg/mL), Listeria monocytogenes (MIC99.9= 4 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 1.3% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 5 and 12) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (5) and Ⓚ (12) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC1C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH3+])CCCC[NH3+])Cc2ccccc2)CCCC[NH2+]CC=CC[NH2+]CCCC1)CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)C([NH3+])CCCC[NH3+]
DRAMP21471	KFFKKLⓀKAVⓀKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 5 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 8 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 8 μg/mL), Listeria monocytogenes (MIC99.9= 2 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 4 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 16 μg/mL)	[Ref.32216308] It has 5.4% hemolysis against red blood cells at peptide concentration of 320 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 7 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (7) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH3+])CCCC[NH3+])Cc2ccccc2)CCCC[NH3+])CCCC[NH2+]CC=CC[NH2+]CCCC1)CC(C)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)C([NH3+])CCCC[NH3+]
DRAMP21472	KFFKKLKⓀAVKⓀGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 6 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 2 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 2.9% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 8 and 12) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (8) and Ⓚ (12) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1C(=O)NC(C)C(=O)NC(C(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH3+])CCCC[NH3+])Cc2ccccc2)CCCC[NH2+]CC=CC[NH2+]CCCC1)CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)C([NH3+])CCCC[NH3+]
DRAMP21473	KFFKKLKⓀAVKKGFⓀKFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 7 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 16 μg/mL), Listeria monocytogenes (MIC99.9= 8 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 16 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 2.6% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 8 and 15) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (8) and Ⓚ (15) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1C(=O)NC(C)C(=O)NC(C(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH3+])CCCC[NH2+]CC=CC[NH2+]CCCC1)CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)C([NH3+])CCCC[NH3+]
DRAMP21474	KFFKKLKKAVⓀKGFⓀKFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 8 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 2 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 2.7% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 11 and 15) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (11) and Ⓚ (15) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC1C(=O)NC(CCCC[NH3+])C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH3+])CCCC[NH2+]CC=CC[NH2+]CCCC1)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])C)C(C)C
DRAMP21475	KFFKKLKKAVKⓀGFKKFAⓀV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 9 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 8 μg/mL), Listeria monocytogenes (MIC99.9= 4 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 16 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 16 μg/mL)	[Ref.32216308] It has 5.4% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 12 and 19) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (12) and Ⓚ (19) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC1C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2ccccc2)C(=O)NC(C)C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH2+]CC=CC[NH2+]CCCC1)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])C)C(C)C
DRAMP21476	KFFKKLKKAVKⓀGFKⓀFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 10 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①41% α-helical content in 30 mM SDS. ②Random coils in PBS	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS.  ②Stapled peptides 10 and 12 had a high content of α-helix of about 41 and 45%, respectively, respectively, which could partly explain their strong antibacterial activity and proteolytic resistance.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 2 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 2.8% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 12 and 16) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (12) and Ⓚ (16) are cross-linked by a (E)-but-2-enyl space employing the N-alkylation reactionr.	L	[Ref.32216308] The cell survial of HEK 293T cell line induced by peptide 10 is 101.8%, 100.7%, 98.9%, 89.1% and 83.9%.	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC1C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH2+]CC=CC[NH2+]CCCC1)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])C)C(C)C
DRAMP21477	KFFKKLKKAVKKGFⓀKFAⓀV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 11 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 8 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 2 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 4 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 16 μg/mL)	[Ref.32216308] It has 0.5% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 15 and 19) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (15) and Ⓚ (19) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC1C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2ccccc2)C(=O)NC(C)C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH2+]CC=CC[NH2+]CCCC1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])C)C(C)C
DRAMP21478	KFFKKLKKAVKⓀGFKⓀFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 12 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①45% α-helical content in 30 mM SDS. ②Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS.  ②Stapled peptides 10 and 12 had a high content of α-helix of about 41 and 45%, respectively, respectively, which could partly explain their strong antibacterial activity and proteolytic resistance.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 2 μg/mL), Listeria monocytogenes (MIC99.9= 4 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 4 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 8 μg/mL)	[Ref.32216308] It has 8.7% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 12 and 16) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (12) and Ⓚ (16) are cross-linked by a 1,2-bismethylenebenzene spacer employing the N-alkylation.	L	[Ref.32216308] The cell survial of HEK 293T cell line induced by peptide 12 is 102.9%, 101.8%, 101.5%, 66.4% and 62.8%.	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC1C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH2+]Cc2c(cccc2)C[NH2+]CCCC1)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])C)C(C)C
DRAMP21479	KFFKKLKKAVKⓀGFKⓀFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 13 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 4 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 6.1% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 12 and 16) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (12) and Ⓚ (16) are cross-linked by a 1,3-bismethylenebenzene spacer employing the N-alkylation.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC1C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH2+]Cc2cc(ccc2)C[NH2+]CCCC1)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])C)C(C)C
DRAMP21480	KFFKKLKKAVKⓀGFKⓀFAKV	KFFKKLKKAVKKGFKKFAKV	KFFKKLKKAVKKGFKKFAKV	20	peptide 14 (derived from OH-CM6)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Random coils in PBS.	①All the peptides were random coils in PBS but displayed varied levels of α-helicity in the presence of 30 mM SDS. ②Other stapled peptides had an α-helix content ranging from 16 to 38%, but their antibacterial activity and proteolytic stability were quite similar.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.32216308] Gram-positive bacteria: Staphylococcus aureus (MIC99.9= 4 μg/mL), methicillin-resistant Staphylococcus aureus (MIC99.9= 4 μg/mL), Listeria monocytogenes (MIC99.9= 4 μg/mL);##Gram-negative bacteria: E.coli (MIC99.9= 8 μg/mL), Pseudomonas aeruginosa (MIC99.9= 8 μg/mL), clinically isolated drug-resistant E.coli (MIC99.9= 32 μg/mL)	[Ref.32216308] It has 6.8% hemolysis against red blood cells at peptide concentration of 320 μg/mL	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 12 and 16) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (12) and Ⓚ (16) are cross-linked by a 1,4-bismethylenebenzene spacer employing the N-alkylation.	L	No cytotoxicity information found in the reference	32216308	J Med Chem. 2020 Apr 23;63(8):4081-4089. doi: 10.1021/acs.jmedchem.9b02025. Epub 2020 Apr 8.	Hong Li, Yuchen Hu, Qi Pu, Tong He, Qianyu Zhang, Wen Wu, Xuefeng Xia and Jinqiang Zhang	Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides	Stapled AMP						O=C(NC(C(=O)NC1C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C(C)C)CCCC[NH3+])C)Cc2ccccc2)CCCC[NH2+]Cc2ccc(cc2)C[NH2+]CCCC1)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCCC[NH3+])Cc1ccccc1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])C)C(C)C
DRAMP21482	KKKKKKAAFⓍAWAⓍFAA	KKKKKKAAFXAWAXFAA	KKKKKKAAFAAWAAFAA	17	S-6K-F17	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		①Random coils with only a small amount of helical structure in aqueous buffer. ②α-helix in SDS detergent micelles.	①Similarly, the stapled peptide, S-6K-F17 is predominantly random coil in aqueous buffer with only a small amount of helical structure despite the presence of the staple - a feature likely due to the large stretch of non-helical Lys residues that flank the stapled portion of the sequence. ②As expected, in detergent micelles S-6K-F17 adopts a helical structure, paralleling the unstapled peptide.	Not found	Function: Antibacterial activity against Gram-negative bacteria. No experiments about antibacterial activity against Gram-positive bacteria are recorded.	[Ref.29275987] Gram-negative bacteria: E. coli (MIC= 1.0 μM)	[Ref.29275987] MHC = 3.8 μM against human red blood cells. Note: Minimum hemolytic concentration (MHC) is the minimum peptide concentration at which red blood cells undergo > 2% hemolysis.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 10 and 14) in sequence indicates 2-(4'-pentenyl) alanine. ②Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	29275987	Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Epub 2017 Oct 21.	Tracy A Stone, Gregory B Cole, Huong Q Nguyen, Simon Sharpe, Charles M Deber	Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C)C)Cc2ccccc2)(C)CCCC=CCCC1)Cc1ccccc1)C)C)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C([NH3+])CCCC[NH3+]
DRAMP21483	KKKKKKAGFⓍAWAⓍFGA	KKKKKKAGFXAWAXFGA	KKKKKKAAFAAWAAFAA	17	S-6K-F17-2G	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		Lack of significant structure	Substitutions with polar, known 'helix-breaker' Gly residues led to losses in helical character until finally the peptide containing 3 Gly and 1 Asn (S-6K-F17-3GN) shows a severe loss in helical structure	Not found	Function: Antibacterial activity against Gram-negative bacteria. No experiments about antibacterial activity against Gram-positive bacteria are recorded.	[Ref.29275987] Gram-negative bacteria: E. coli (MIC= 1.6 μM)	[Ref.29275987] MHC = 15 μM against human red blood cells. Note: Minimum hemolytic concentration (MHC) is the minimum peptide concentration at which red blood cells undergo > 2% hemolysis.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 10 and 14) in sequence indicates 2-(4'-pentenyl) alanine. ②Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	29275987	Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Epub 2017 Oct 21.	Tracy A Stone, Gregory B Cole, Huong Q Nguyen, Simon Sharpe, Charles M Deber	Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC1(C)C(=O)NC(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C=O)C)Cc2ccccc2)(C)CCCC=CCCC1)Cc1ccccc1)C)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C([NH3+])CCCC[NH3+]
DRAMP21484	KKKKKKAGFⓍAWGⓍFGA	KKKKKKAGFXAWGXFGA	KKKKKKAAFAAWAAFAA	17	S-6K-F17-3G	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		Lack of significant structure	Substitutions with polar, known 'helix-breaker' Gly residues led to losses in helical character until finally the peptide containing 3 Gly and 1 Asn (S-6K-F17-3GN) shows a severe loss in helical structure	Not found	Function: Antibacterial activity against Gram-negative bacteria. No experiments about antibacterial activity against Gram-positive bacteria are recorded.	[Ref.29275987] Gram-negative bacteria: E. coli (MIC= 4.2 μM)	[Ref.29275987] MHC = 128 μM against human red blood cells. Note: Minimum hemolytic concentration (MHC) is the minimum peptide concentration at which red blood cells undergo > 2% hemolysis.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 10 and 14) in sequence indicates 2-(4'-pentenyl) alanine. ②Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	29275987	Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Epub 2017 Oct 21.	Tracy A Stone, Gregory B Cole, Huong Q Nguyen, Simon Sharpe, Charles M Deber	Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC1(C)C(=O)NC(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NCC(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C=O)C)Cc2ccccc2)(C)CCCC=CCCC1)Cc1ccccc1)C)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C([NH3+])CCCC[NH3+]
DRAMP21485	KKKKKKNGFⓍAWGⓍFGA	KKKKKKNGFXAWGXFGA	KKKKKKAAFAAWAAFAA	17	S-6K-F17-3GN	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		Lack of significant structure	Substitutions with polar, known 'helix-breaker' Gly residues led to losses in helical character until finally the peptide containing 3 Gly and 1 Asn (S-6K-F17-3GN) shows a severe loss in helical structure	Not found	Function: Antibacterial activity against Gram-negative bacteria. No experiments about antibacterial activity against Gram-positive bacteria are recorded.	[Ref.29275987] Gram-negative bacteria: E. coli (MIC= 4.2 μM)	[Ref.29275987] MHC = 587 μM against human red blood cells. Note: Minimum hemolytic concentration (MHC) is the minimum peptide concentration at which red blood cells undergo > 2% hemolysis.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 10 and 14) in sequence indicates 2-(4'-pentenyl) alanine. ②Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	29275987	Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Epub 2017 Oct 21.	Tracy A Stone, Gregory B Cole, Huong Q Nguyen, Simon Sharpe, Charles M Deber	Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC1(C)C(=O)NC(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NCC(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C=O)C)Cc2ccccc2)(C)CCCC=CCCC1)Cc1ccccc1)CC(=O)N)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C([NH3+])CCCC[NH3+]
DRAMP21486	VNWKKⓍLGKⓍIKVVK	VNWKKXLGKXIKVVK	VNWKKILGKIIKVVK	15	LL-IIIs-1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal		①20% α-helical content in water. ②55% α-helical content in 50% TFE. ③55% α-helical content in 8mM SDS.	It seems that the staple in the central part of the LL-IIIs-1 analog that crosslink the bend of the α-helix on its concave site around the Gly8 residue resulted in slight helix destabilization.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 0.7 μM), Bacillus subtilis (MIC = 0.8 μM), Staphylococcus aureus (MIC = 12.5 μM);##Gram-negative bacteria: E.coli (MIC = 4.4 μM), Pseudomonas aeruginosa (MIC = 78.7 μM);##Fungi: Candida albicans (MIC = 100 μM).	[Ref.22526241] LC50 = 31.3 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 6 and 10) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 18.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NCC(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C(C)C)C(C)C)CCCC[NH3+])C(CC)C)(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])Cc1c2c([nH]c1)cccc2)CC(=O)N)C([NH3+])C(C)C
DRAMP21487	VNWKKILGKⓍIKVⓍK	VNWKKILGKXIKVXK	VNWKKILGKIIKVVK	15	LL-IIIs-2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal		①31% α-helical content in water. ②51% α-helical content in 50% TFE. ③58% α-helical content in 8mM SDS.	For the LL-IIIs-2 analog, the helical content increment is slightly higher (8 %).	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 0.9 μM), Bacillus subtilis (MIC = 1.2 μM), Staphylococcus aureus (MIC = 20.3 μM);##Gram-negative bacteria: E.coli (MIC = 8.8 μM), Pseudomonas aeruginosa (MIC = 86.7 μM);##Fungi: Candida albicans (MIC = 100 μM).	[Ref.22526241] LC50 = 69 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (10) and Ⓧ (14)are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 19.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC1(C)C(=O)NC(C(CC)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CC(C)C)C(CC)C)CCCC[NH3+])CCCC[NH3+])Cc1c2c([nH]c1)cccc2)CC(=O)N)C([NH3+])C(C)C
DRAMP21488	VⓍWKKⓍLGKIIKVVK	VXWKKXLGKIIKVVK	VNWKKILGKIIKVVK	15	LL-IIIs-3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal		①27% α-helical content in water. ②52% α-helical content in 50% TFE. ③62% α-helical content in 8mM SDS.	The CD spectra of the singly stapled peptides of the i, i + 4 type acquired in water show a slight increase (by 5 %) of helical content in the case of MEP-Ns-1, MEP-Ns-2 and LL-IIIs-3 compared to their unstapled precursors.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.4 μM), Bacillus subtilis (MIC = 1.1 μM), Staphylococcus aureus (MIC = 21.7 μM);##Gram-negative bacteria: E.coli (MIC = 1.2 μM), Pseudomonas aeruginosa (MIC = 76.3 μM);##Fungi: Candida albicans (MIC = 93.3 μM).	[Ref.22526241] LC50 = 30 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 20.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C(C)C)C(C)C)CCCC[NH3+])C(CC)C)C(CC)C)CCCC[NH3+])CC(C)C)(C)CCCC=CCCC1)C([NH3+])C(C)C
DRAMP21489	VNⓍKKIⓍGKⓍIKVⓍK	VNXKKIXGKXIKVXK	VNWKKILGKIIKVVK	15	LL-IIIs-4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①45% α-helical content in water. ②48% α-helical content in 50% TFE. ③63% α-helical content in 8mM SDS.	On the other hand, the difference in α-helical content between doubly stapled analogs (LL-IIIs-4, MEP-Ns-3, MEP-Ns-5, and MEP-Ns-6) and their unstapled precursors is apparently higher, on average by 15 %	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 2 μM), Bacillus subtilis (MIC = 1.1 μM), Staphylococcus aureus (MIC = 80 μM);##Gram-negative bacteria: E.coli (MIC = 20 μM), Pseudomonas aeruginosa (MIC > 100 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 > 100 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 3, 7, 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (3) and Ⓧ (7), Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 21.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC1(C)C(=O)NC(C(CC)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])C)C(CC)C)CCCC[NH3+])CCCC[NH3+])C)CC(=O)N)C([NH3+])C(C)C
DRAMP21490	VNⓏKKILGKⓍIKVVK	VNZKKILGKXIKVVK	VNWKKILGKIIKVVK	15	LL-IIIs-5 cis	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①22% α-helical content in water. ②54% α-helical content in 50% TFE. ③69% α-helical content in 8mM SDS.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 0.9 μM), Bacillus subtilis (MIC = 0.9 μM), Staphylococcus aureus (MIC = 45 μM);##Gram-negative bacteria: E.coli (MIC = 3.5 μM), Pseudomonas aeruginosa (MIC = 80 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 = 100 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓩ (position: 3) indicates 2-(7'-octenyl) alanine in the R configuration. ②The Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. ③Ⓩ (3) and Ⓧ (10) are cross-linked by hydrocarbon stapling.	L, cis	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 22.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(CC)C)C(=O)NC(CC(C)C)C(=O)NCC(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C(C)C)C(C)C)CCCC[NH3+])C(CC)C)(C)CCCC=CCCCCCC1)CC(=O)N)C([NH3+])C(C)C
DRAMP21491	VNⓏKKILGKⓍIKVVK	VNZKKILGKXIKVVK	VNWKKILGKIIKVVK	15	LL-IIIs-5 trans	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①26% α-helical content in water. ②54% α-helical content in 50% TFE. ③62% α-helical content in 8mM SDS.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.1 μM), Bacillus subtilis (MIC = 1.3 μM), Staphylococcus aureus (MIC = 65 μM);##Gram-negative bacteria: E.coli (MIC = 5.5 μM), Pseudomonas aeruginosa (MIC = 80 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 > 100 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓩ (position: 3) indicates 2-(7'-octenyl) alanine in the R configuration. ②The Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. ③Ⓩ (3) and Ⓧ (10) are cross-linked by hydrocarbon stapling.	L, trans	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 23.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(CC)C)C(=O)NC(CC(C)C)C(=O)NCC(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C(C)C)C(C)C)CCCC[NH3+])C(CC)C)(C)CCCC=CCCCCCC1)CC(=O)N)C([NH3+])C(C)C
DRAMP21492	VNⓍKKIⓍPKⓍIKVⓍK	VNXKKIXPKXIKVXK	VNWKKILGKIIKVVK	15	LL-IIIs-6a	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①36% α-helical content in water. ②42% α-helical content in 50% TFE. ③36% α-helical content in 8mM SDS.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1 μM), Bacillus subtilis (MIC = 1.1 μM), Staphylococcus aureus (MIC = 93 μM);##Gram-negative bacteria: E.coli (MIC = 7.8 μM), Pseudomonas aeruginosa (MIC = 93 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 > 100 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 3, 7, 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (3) and Ⓧ (7), Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling respectively.	L, cis(around the S₅-Pro8 peptide bond)	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 24.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(CC)C)C(=O)NC(C(=O)N2C(C(=O)NC(C(=O)NC3(C)C(=O)NC(C(CC)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC3)CCCC[NH3+])CCC2)(C)CCCC=CCCC1)CC(=O)N)C([NH3+])C(C)C
DRAMP21493	VNⓍKKIⓍPKⓍIKVⓍK	VNXKKIXPKXIKVXK	VNWKKILGKIIKVVK	15	LL-IIIs-6b	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①33% α-helical content in water. ②38% α-helical content in 50% TFE. ③35% α-helical content in 8mM SDS.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 0.9 μM), Bacillus subtilis (MIC = 0.8 μM), Staphylococcus aureus (MIC = 50 μM);##Gram-negative bacteria: E.coli (MIC = 7.8 μM), Pseudomonas aeruginosa (MIC = 63 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 = 82μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 3, 7, 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (3) and Ⓧ (7), Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling respectively.	L, trans(around the S₅-Pro8 peptide bond)	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 25.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						
DRAMP21495	GFLSILKKVLPKⓍJAHⓍK	GFLSILKKVLPKXJAHXK	GFLSILKKVLPKVMAHMK	18	MEP-Ns-1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal		①19% α-helical content in water.②66% α-helical content in 50% TFE. ③75% α-helical content in 8mM SDS.	The CD spectra of the singly stapled peptides of the i, i + 4 type acquired in water show a slight increase (by 5 %) of helical content in the case of MEP-Ns-1, MEP-Ns-2 and LL-IIIs-3 compared to their unstapled precursors.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 0.8 μM), Bacillus subtilis (MIC = 1.1 μM), Staphylococcus aureus (MIC = 10.8 μM);##Gram-negative bacteria: E.coli (MIC = 2.5 μM), Pseudomonas aeruginosa (MIC = 77 μM);##Fungi: Candida albicans (MIC = 30 μM).	[Ref.22526241] LC50 = 18.1 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The J (position: 14) in sequence indicates norleucine. ②The Ⓧ (position: 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 28.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)N1C(C(=O)NC(C(=O)NC2(C)C(=O)NC(CCCC)C(=O)NC(C)C(=O)NC(Cc3nc[nH]c3)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC2)CCCC[NH3+])CCC1)CC(C)C)C(C)C)CCCC[NH3+])CCCC[NH3+])CC(C)C)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C[NH3+])Cc1ccccc1)CC(C)C)CO)C(CC)C
DRAMP21496	GFLSⓍLKKⓍLPKVJAHJK	GFLSXLKKXLPKVJAHJK	GFLSILKKVLPKVMAHMK	18	MEP-Ns-2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①16% α-helical content in water.②61% α-helical content in 50% TFE. ③62% α-helical content in 8mM SDS.	The CD spectra of the singly stapled peptides of the i, i + 4 type acquired in water show a slight increase (by 5 %) of helical content in the case of MEP-Ns-1, MEP-Ns-2 and LL-IIIs-3 compared to their unstapled precursors.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.5 μM), Bacillus subtilis (MIC = 1.2 μM), Staphylococcus aureus (MIC = 37 μM);##Gram-negative bacteria: E.coli (MIC = 7.8 μM), Pseudomonas aeruginosa (MIC ≥ 100 μM);##Fungi: Candida albicans (MIC ≥ 100 μM).	[Ref.22526241] LC50 = 14.7 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The J (position: 14 and 17) in sequence indicates norleucine. ②The Ⓧ (position: 5 and 9) indicates 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (5) and Ⓧ (9) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 29.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C)Cc1nc[nH]c1)C)CCCC)C(NC(=O)C(NC(=O)C1N(C(=O)C(NC(=O)C2(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C[NH3+])Cc3ccccc3)CC(C)C)CO)(C)CCCC=CCCC2)CC(C)C)CCC1)CCCC[NH3+])C(C)C
DRAMP21497	GFLSⓍLKKⓍLPKⓍJAHⓍK	GFLSXLKKXLPKXJAHXK	GFLSILKKVLPKVMAHMK	18	MEP-Ns-3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①34% α-helical content in water.②56% α-helical content in 50% TFE. ③48% α-helical content in 8mM SDS.	On the other hand, the difference in α-helical content between doubly stapled analogs (LL-IIIs-4, MEP-Ns-3, MEP-Ns-5, and MEP-Ns-6) and their unstapled precursors is apparently higher, on average by 15 %	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC =  1.3 μM), Bacillus subtilis (MIC = 1.2 μM), Staphylococcus aureus (MIC ≥ 100 μM);##Gram-negative bacteria: E.coli (MIC = 46.7 μM), Pseudomonas aeruginosa (MIC > 100 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 = 13.9 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The J (position: 14) in sequence indicates norleucine. ②Ⓧ (position: 5, 9, 13 and 17) are 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 30.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)N2C(C(=O)NC(C(=O)NC3(C)C(=O)NC(CCCC)C(=O)NC(C)C(=O)NC(Cc4nc[nH]c4)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC3)CCCC[NH3+])CCC2)CC(C)C)(C)CCCC=CCCC1)CO)C(NC(=O)C(NC(=O)C[NH3+])Cc1ccccc1)CC(C)C
DRAMP21498	GFⓏSILKKVⓍPKVJAHJK	GFZSILKKVXPKVJAHJK	GFLSILKKVLPKVMAHMK	18	MEP-Ns-4 cis	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Unknown	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.5 μM), Bacillus subtilis (MIC = 1.3 μM), Staphylococcus aureus (MIC = 37 μM);##Gram-negative bacteria: E.coli (MIC = 8.1 μM), Pseudomonas aeruginosa (MIC ≥ 100 μM);##Fungi: Candida albicans (MIC ≥ 100 μM).	[Ref.22526241] LC50 = 11 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The J (position: 14 and 17) in sequence indicates norleucine. ②Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. ③Ⓩ (position: 3) is 2-(7'-pctenyl) lalnine in the R configuration. ④Ⓧ (10) and Ⓩ (3) are cross-linked by hydrocarbon stapling.	L, cis	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 31.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])CCCC)Cc1nc[nH]c1)C)C)C(NC(=O)C(NC(=O)C1N(C(=O)C2(C)NC(=O)C(C(C)C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(CC(C)C)NC(=O)C(C(CC)C)NC(=O)C(CO)NC(=O)C(NC(=O)C(NC(=O)C[NH3+])Cc3ccccc3)(C)CCCCCCC=CCCC2)CCC1)CCCC[NH3+])C(C)C
DRAMP21499	GFⓏSILKKVⓍPKVJAHJK	GFZSILKKVXPKVJAHJK	GFLSILKKVLPKVMAHMK	18	MEP-Ns-4 trans	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Unknown	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 2 μM), Bacillus subtilis (MIC = 1.7 μM), Staphylococcus aureus (MIC = 63 μM);##Gram-negative bacteria: E.coli (MIC = 16.3 μM), Pseudomonas aeruginosa (MIC ≥ 100 μM);##Fungi: Candida albicans (MIC ≥ 100 μM).	[Ref.22526241] LC50 = 20 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The J (position: 14 and 17) in sequence indicates norleucine. ②Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. ③Ⓩ (position: 3) is 2-(7'-pctenyl) lalnine in the R configuration. ④Ⓧ (10) and Ⓩ (3) are cross-linked by hydrocarbon stapling.	L, trans	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 32.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])CCCC)Cc1nc[nH]c1)C)CCCC)C(NC(=O)C(NC(=O)C1N(C(=O)C2(C)NC(=O)C(C(C)C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(CC(C)C)NC(=O)C(C(CC)C)NC(=O)C(CO)NC(=O)C(NC(=O)C(NC(=O)C[NH3+])Cc3ccccc3)(C)CCCCCCC=CCCC2)CCC1)CCCC[NH3+])C(C)C
DRAMP21500	GFLSⓍLKKⓍLGKⓍJAHⓍK	GFLSXLKKXLGKXJAHXK	GFLSILKKVLPKVMAHMK	18	MEP-Ns-5	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①52% α-helical content in water.②67% α-helical content in 50% TFE. ③59% α-helical content in 8mM SDS.	On the other hand, the difference in α-helical content between doubly stapled analogs (LL-IIIs-4, MEP-Ns-3, MEP-Ns-5, and MEP-Ns-6) and their unstapled precursors is apparently higher, on average by 15 %	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.5 μM), Bacillus subtilis (MIC = 1.2 μM), Staphylococcus aureus (MIC = 57 μM);##Gram-negative bacteria: E.coli (MIC = 5.6 μM), Pseudomonas aeruginosa (MIC > 100 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 = 29 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The J (position: 14) in sequence indicates norleucine. ②Ⓧ (position: 5, 9, 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 33.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC2(C)C(=O)NC(CCCC)C(=O)NC(C)C(=O)NC(Cc3nc[nH]c3)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC2)CCCC[NH3+])CC(C)C)(C)CCCC=CCCC1)CO)C(NC(=O)C(NC(=O)C[NH3+])Cc1ccccc1)CC(C)C
DRAMP21501	GFLSⓍLKKⓍLAKⓍJAHⓍK	GFLSXLKKXLAKXJAHXK	GFLSILKKVLPKVMAHMK	18	MEP-Ns-6	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①56% α-helical content in water.②64% α-helical content in 50% TFE. ③56% α-helical content in 8mM SDS.	On the other hand, the difference in α-helical content between doubly stapled analogs (LL-IIIs-4, MEP-Ns-3, MEP-Ns-5, and MEP-Ns-6) and their unstapled precursors is apparently higher, on average by 15 %	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.	[Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.5 μM), Bacillus subtilis (MIC = 1.2 μM), Staphylococcus aureus (MIC = 43 μM);##Gram-negative bacteria: E.coli (MIC = 5.6 μM), Pseudomonas aeruginosa (MIC > 100 μM);##Fungi: Candida albicans (MIC > 100 μM).	[Ref.22526241] LC50 = 39.5 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.	Cyclic (Stapled)	Free	Amidation	①The J (position: 14) in sequence indicates norleucine. ②Ⓧ (position: 5, 9, 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	22526241	Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 34.	Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský	Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera	Stapled AMP						O=C(NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2(C)C(=O)NC(CCCC)C(=O)NC(C)C(=O)NC(Cc3nc[nH]c3)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC2)CCCC[NH3+])C)CC(C)C)(C)CCCC=CCCC1)CO)C(NC(=O)C(NC(=O)C[NH3+])Cc1ccccc1)CC(C)C
DRAMP21502	IDWKKLLⓀAAKⒼIL	IDWKKLLKAAKGIL	IDWKKLLDAAKQIL	14	C-MP1-1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①Slight α-helical structure in aqueous solution. ②Increased α-helical conformation in 30 mM SDS and 50% TFE compared with MPI	①By CD, we observed that C-MPI-2 and MPI did not display any structural preferences in aqueous solution, whereas C-MPI-1 adopoted a slight α-helical structure. ②C-MPI-1 also had higher α-helicity than MPI in membrane mimicking environments, including 30 mM sodium dodecyl sulfate (SDS) and 50% trifluoroethyl alcohol (TFE).	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28833783] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 64 μM), Bacillus subtilis ATCC 23857 (MIC = 8 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 64 μM), Pseudomonas aeruginosa ATCC 27853 (No antimicrobial activity)	[Ref.28833783] It has 0%, 0%, 2.1%, 9.5%, 22.7%, 25.4% and 34.7% against human red blood cells at peptide concentrations of 0, 5, 10, 25, 50, 75 and 150 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓚ (position: 8) is lysine with the methyltrityl side chain. ②The Ⓖ (position: 12) is propargylglycine. ③Ⓚ (8) and Ⓖ (12) are cross-linked by hydrocarbon stapling by 1,3-diploar azide-alkyne cyclization.	L	No cytotoxicity information found in the reference	28833783	J Pept Sci. 2017 Nov;23(11):824-832. doi: 10.1002/psc.3031. Epub 2017 Aug 23.	Beijun Liu, Wei Zhang, Sanhu Gou, Haifeng Huang, Jia Yao, Zhibin Yang, Hui Liu, Chao Zhong, Beiyin Liu, Jingman Ni, Rui Wang	Intramolecular cyclization of the antimicrobial peptide Polybia-MPI with triazole stapling: influence on stability and bioactivity	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CC(C)C)C(CC)C)CC=N)CCCC[NH3+])C)C)CCCC[NH3+])CC(C)C)CC(C)C)CCCC[NH3+])CCCC[NH3+])Cc1c2c([nH]c1)cccc2)CC(=O)[O-])C([NH3+])C(CC)C.[H+H0]
DRAMP21503	IⓀWKKLLⒼAAKQIL	IKWKKLLGAAKQIL	IDWKKLLDAAKQIL	14	C-MP1-2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No structural preference in aqueous solution.	By CD, we observed that C-MPI-2 and MPI did not display any structural preferences in aqueous solution, whereas C-MPI-1 adopoted a slight α-helical structure.	Not found	Function: Antibacterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria is not so evident.	[Ref.28833783] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 256 μM), Bacillus subtilis ATCC 23857 (MIC = 128 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 128 μM), Pseudomonas aeruginosa ATCC 27853 (No antimicrobial activity)	[Ref.28833783] No hemolytic information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓚ (position: 2) is lysine with the methyltrityl side chain. ②The Ⓖ (position: 8) is propargylglycine. ③Ⓚ (2) and Ⓖ (8) are cross-linked by hydrocarbon stapling by 1,3-diploar azide-alkyne cyclization.	L	No cytotoxicity information found in the reference	28833783	J Pept Sci. 2017 Nov;23(11):824-832. doi: 10.1002/psc.3031. Epub 2017 Aug 23.	Beijun Liu, Wei Zhang, Sanhu Gou, Haifeng Huang, Jia Yao, Zhibin Yang, Hui Liu, Chao Zhong, Beiyin Liu, Jingman Ni, Rui Wang	Intramolecular cyclization of the antimicrobial peptide Polybia-MPI with triazole stapling: influence on stability and bioactivity	Stapled AMP						O=C(NC1C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CC(C)C)C(CC)C)CCC(=O)N)CCCC[NH3+])C)C)CC[NH2+]CCCC1)C([NH3+])C(CC)C.[NH4+].[H+H0]
DRAMP21504	ⓍIGKⓍLHSAKKFGKAFVGEIJNS	XIGKXLHSAKKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)0	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		15% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 59.46 μg/mL), Bacillus cereus ATCC 14579 (MIC = 10.49 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 25.00 μg/mL)	[Ref.31427820] It has 5.6% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 1 and 5) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (1) and Ⓧ (5) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(C(CC)C)NC(=O)C([NH3+])(C)CCCC=CCCC1)CC(C)C)Cc1[nH]cnc1)CO)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21505	GⓍGKFⓍHSAKKFGKAFVGEIJNS	GXGKFXHSAKKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		12% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 100.00 μg/mL), Bacillus cereus ATCC 14579 (MIC = 14.87 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.72 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 12.50 μg/mL)	[Ref.31427820] It has 4.6% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(NC(=O)C[NH3+])(C)CCCC=CCCC1)Cc1nc[nH]c1)CO)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21506	GIⓍKFLⓍSAKKFGKAFVGEIJNS	GIXKFLXSAKKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		21% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 12.50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 7.43 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 10.51 μg/mL)	[Ref.31427820] It has 18.3% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 3 and 7) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (3) and Ⓧ (7) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C[NH3+])C(CC)C)(C)CCCC=CCCC1)CO)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21507	GIGⓍFLHⓍAKKFGKAFVGEIJNS	GIGXFLHXAKKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		18% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 8.84 μg/mL), Bacillus cereus ATCC 14579 (MIC = 10.51 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 7.43 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 25.00 μg/mL)	[Ref.31427820] It has 42.1% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 4 and 8) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (4) and Ⓧ (8) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(Cc2[nH]cnc2)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)(C)CCCC=CCCC1)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21508	GIGKⓍLHSⓍKKFGKAFVGEIJNS	GIGKXLHSXKKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		24% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 25.00 μg/mL), Bacillus cereus ATCC 14579 (MIC = 6.25 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 4.42 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 10.51 μg/mL)	[Ref.31427820] It has 18.3% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 5 and 9) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (5) and Ⓧ (9) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CO)NC(=O)C(Cc2[nH]cnc2)NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21509	GIGKFⓍHSAⓍKFGKAFVGEIJNS	GIGKFXHSAXKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)5	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		14% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 25.00 μg/mL), Bacillus cereus ATCC 14579 (MIC = 17.68 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 14.87 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 50.00 μg/mL)	[Ref.31427820] It has 13.2% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C)NC(=O)C(CO)NC(=O)C(Cc2[nH]cnc2)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)(C)CCCC=CCCC1)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21510	GIGKFLⓍSAKⓍFGKAFVGEIJNS	GIGKFLXSAKXFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)6	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		18% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 25.00 μg/mL), Bacillus cereus ATCC 14579 (MIC = 12.50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 7.43 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 29.73 μg/mL)	[Ref.31427820] It has 7.6% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 7 and 11) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (7) and Ⓧ (11) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(C)NC(=O)C(CO)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)(C)CCCC=CCCC1)Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21511	GIGKFLHⓍAKKⓍGKAFVGEIJNS	GIGKFLHXAKKXGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)7	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		26% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 6.25 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.72 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.63 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 6.25 μg/mL)	[Ref.31427820] It has 62.4% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 8 and 12) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (8) and Ⓧ (12) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)(C)CCCC=CCCC1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21512	GIGKFLHSⓍKKFⓍKAFVGEIJNS	GIGKFLHSXKKFXKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)8	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		49% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 7.44 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.26 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.63 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.72 μg/mL)	[Ref.31427820] It has 74.6% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 9 and 13) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)(C)CCCC=CCCC1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21513	GIGKFLHSAⓍKFGⓍAFVGEIJNS	GIGKFLHSAXKFGXAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)9	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		28% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 17.68 μg/mL), Bacillus cereus ATCC 14579 (MIC = 12.50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 4.42 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 59.46 μg/mL)	[Ref.31427820] It has 60.0% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 10 and 14) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)C)(C)CCCC=CCCC1)C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21514	GIGKFLHSAKⓍFGKⓍFVGEIJNS	GIGKFLHSAKXFGKXFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)10	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		15% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 8.84 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.42 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 4.42 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 14.87 μg/mL)	[Ref.31427820] It has 23.9% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 11 and 15) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (11) and Ⓧ (15) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2nc[nH]c2)CO)C)CCCC[NH3+])(C)CCCC=CCCC1)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21515	GIGKFLHSAKKⓍGKAⓍVGEIJNS	GIGKFLHSAKKXGKAXVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)11	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		16% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 12.50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.26 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 8.84 μg/mL)	[Ref.31427820] It has 17.8% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (12) and Ⓧ (16) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C1(C)NC(=O)C(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)C)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21516	GIGKFLHSAKKFⓍKAFⓍGEIJNS	GIGKFLHSAKKFXKAFXGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)12	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		51% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 7.43 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.72 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.63 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 4.42 μg/mL)	[Ref.31427820] It has 76.6% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 13 and 17) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C1(C)NC(=O)C(Cc2ccccc2)NC(=O)C(C)NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)C)CCCC[NH3+])CCCC[NH3+])Cc2ccccc2)(C)CCCC=CCCC1)CCC(=O)[O-])C(CC)C
DRAMP21517	GIGKFLHSAKKFGⓍAFVⓍEIJNS	GIGKFLHSAKKFGXAFVXEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)13	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		23% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 5.26 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.72 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 7.43 μg/mL)	[Ref.31427820] It has 60.0% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 14 and 18) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (14) and Ⓧ (18) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)C)CCCC[NH3+])CCCC[NH3+])Cc2ccccc2)(C)CCCC=CCCC1)CCC(=O)[O-])C(CC)C
DRAMP21518	GIGKFLHSAKKFGKⓍFVGⓍIJNS	GIGKFLHSAKKFGKXFVGXIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)14	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		19% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 2.63 μg/mL), Bacillus cereus ATCC 14579 (MIC = 2.63 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.86 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.13 μg/mL)	[Ref.31427820] It has 92.4% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 15 and 19) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (15) and Ⓧ (19) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C1(C)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)C)CCCC[NH3+])CCCC[NH3+])Cc2ccccc2)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C
DRAMP21519	GIGKFLHSAKKFGKAⓍVGEⓍJNS	GIGKFLHSAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)15	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		15% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 10.51 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.26 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.63 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 7.43 μg/mL)	[Ref.31427820] It has 11.7% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21520	GIGKFLHSAKKFGKAFⓍGEIⓍNS	GIGKFLHSAKKFGKAFXGEIXNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)16	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		11% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 42.04 μg/mL), Bacillus cereus ATCC 14579 (MIC = 7.44 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.72 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 8.84 μg/mL)	[Ref.31427820] It has 8.1% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 17 and 21) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (17) and Ⓧ (21) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(CC)C)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)(C)CCCC=CCCC1)Cc1ccccc1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21521	GIGKFLHSAKKFGKAFVⓍEIJⓍS	GIGKFLHSAKKFGKAFVXEIJXS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)17	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		30% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 2.63 μg/mL), Bacillus cereus ATCC 14579 (MIC = 1.86 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.56 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 5.26 μg/mL)	[Ref.31427820] It has 56.3% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 18 and 22) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (18) and Ⓧ (22) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCC(=O)[O-])C(=O)NC(C(CC)C)C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CO)(C)CCCC=CCCC1)C(C)C)Cc1ccccc1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21522	GIGKFLHSAKKFGKAFVGⓍIJNⓍ	GIGKFLHSAKKFGKAFVGXIJNX	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(I+4)18	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		19% α-helical content in 25-50 μM potassium phosphate solution.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 1.56 μg/mL), Bacillus cereus ATCC 14579 (MIC = 2.21 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.56 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 2.21 μg/mL)	[Ref.31427820] It has 101.0% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 19 and 23) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (19) and Ⓧ (23) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC1(C)C(=O)NC(C(CC)C)C(=O)NC(CCCC)C(=O)NC(CC(=O)N)C(=O)NC(C=O)(C)CCCC=CCCC1)C(C)C)Cc1ccccc1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1nc[nH]c1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21523	KIGKFLHSAKKFGKAⓍVGEⓍJNS	KIGKFLHSAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(G1K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 21.02 μg/mL), Bacillus cereus ATCC 14579 (MIC = 10.49 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 5.41 μg/mL)	[Ref.31427820] It has 4.4% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C([NH3+])CCCC[NH3+])C(CC)C
DRAMP21524	GKGKFLHSAKKFGKAⓍVGEⓍJNS	GKGKFLHSAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(I2K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 35.36 μg/mL), Bacillus cereus ATCC 14579 (MIC = 25.00 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 4.75 μg/mL)	[Ref.31427820] It has 2.2% hemolysis against human red blood cells at 25 μg/mL..	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CC(C)C)Cc1[nH]cnc1)CO
DRAMP21525	GIKKFLHSAKKFGKAⓍVGEⓍJNS	GIKKFLHSAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(G3K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 10.49 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.21 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.34 μg/mL)	[Ref.31427820] It has 3.7% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21526	GIGKKLHSAKKFGKAⓍVGEⓍJNS	GIGKKLHSAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(F5K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 50 μg/mL.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC > 50 μg/mL), Bacillus cereus ATCC 14579 (MIC > 50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.69 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 17.68 μg/mL)	[Ref.31427820] It has 1.5% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21527	GIGKFKHSAKKFGKAⓍVGEⓍJNS	GIGKFKHSAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(L6K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 50 μg/mL.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC > 50 μg/mL), Bacillus cereus ATCC 14579 (MIC > 50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.63 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 17.68 μg/mL)	[Ref.31427820] It has 1.7% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1nc[nH]c1)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21528	GIGKFLKSAKKFGKAⓍVGEⓍJNS	GIGKFLKSAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(H7K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 6.20 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.21 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 2.69 μg/mL)	[Ref.31427820] It has 3.1% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)CCCC[NH3+])CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21529	GIGKFLHKAKKFGKAⓍVGEⓍJNS	GIGKFLHKAKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(S8K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 6.20 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.38 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 2.65 μg/mL)	[Ref.31427820] It has 3.3% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CCCC[NH3+])Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21530	GIGKFLHSKKKFGKAⓍVGEⓍJNS	GIGKFLHSKKKFGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(A9K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 50 μg/mL.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC > 50 μg/mL), Bacillus cereus ATCC 14579 (MIC > 50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 4.38 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 15.81 μg/mL)	[Ref.31427820] It has 1.7% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21531	GIGKFLHSAKKKGKAⓍVGEⓍJNS	GIGKFLHSAKKKGKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(F12K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 50 μg/mL.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC > 50 μg/mL), Bacillus cereus ATCC 14579 (MIC > 50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.63 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 14.03 μg/mL)	[Ref.31427820] It has 1.9% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21532	GIGKFLHSAKKFKKAⓍVGEⓍJNS	GIGKFLHSAKKFKKAXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(G13K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 50 μg/mL.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC > 50 μg/mL), Bacillus cereus ATCC 14579 (MIC > 50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.10 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 12.82 μg/mL)	[Ref.31427820] It has 1.8% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21533	GIGKFLHSAKKFGKKⓍVGEⓍJNS	GIGKFLHSAKKFGKKXVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(A15K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 31.50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 9.89 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.10 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 4.97 μg/mL)	[Ref.31427820] It has 6.5% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21534	GIGKFLHSAKKFGKAⓍKGEⓍJNS	GIGKFLHSAKKFGKAXKGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(V17K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC > 50 μg/mL), Bacillus cereus ATCC 14579 (MIC > 50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.91 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 19.84 μg/mL)	[Ref.31427820] It has 2.1% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21535	GIGKFLHSAKKFGKAⓍVKEⓍJNS	GIGKFLHSAKKFGKAXVKEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(G18K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 8.80 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.38 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.23 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.57 μg/mL)	[Ref.31427820] It has 8.3% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21536	GIGKFLHSAKKFGKAⓍVGKⓍJNS	GIGKFLHSAKKFGKAXVGKXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(E19K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 25.00 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.21 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 2.23 μg/mL)	[Ref.31427820] It has 6.0% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21537	GIGKFLHSAKKFGKAⓍVGEⓍKNS	GIGKFLHSAKKFGKAXVGEXKNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(B21K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC > 50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 29.73 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.23 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 8.97 μg/mL)	[Ref.31427820] It has 3.2% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC[NH3+])(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21538	GIGKFLHSAKKFGKAⓍVGEⓍJKS	GIGKFLHSAKKFGKAXVGEXJKS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(N22K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 21.02 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.38 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.60 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.57 μg/mL)	[Ref.31427820] It has 11.9% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CCCC[NH3+])CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21539	GIGKFLHSAKKFGKAⓍVGEⓍJNK	GIGKFLHSAKKFGKAXVGEXJNK	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)15(S23K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 42.04 μg/mL), Bacillus cereus ATCC 14579 (MIC = 7.39 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.23 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.57 μg/mL)	[Ref.31427820] It has 4.9% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The J (position: 21) in sequence is norlercine. ③Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])CC(=O)N)CCCC)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21540	GⓍGSFⓍKKKAHVGKHⓍGKAⓍLTHYL	GXGSFXKKKAHVGKHXGKAXLTHYL	GWGSFFKKAAHVGKHVGKAALTHYL	25	Pleu(i+4)1,15(A9K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 3.13 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.13 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.56 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 1.56 μg/mL)	[Ref.31427820] It has 17.1% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2, 6, 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CC(C)C)Cc1ccc(O)cc1)Cc1nc[nH]c1)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C2(C)NC(=O)C(Cc3ccccc3)NC(=O)C(CO)NC(=O)CNC(=O)C(NC(=O)C[NH3+])(C)CCCC=CCCC2)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C)Cc2[nH]cnc2)C(C)C)CCCC[NH3+])Cc2nc[nH]c2)(C)CCCC=CCCC1)CC(C)C)C(O)C
DRAMP21541	GⓍRKRⓍRKFRNKIKEKKKKIGQKⓍQGLⓍPKLA	GXRKRXRKFRNKIKEKKKKIGQKXQGLXPKLA	GLRKRLRKFRNKIKEKLKKIGQKIQGFVPKLAPRTDY	32	CAP(i+4)1,23(L17K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 12.5 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.13 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.56 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 1.56 μg/mL)	[Ref.31427820] It has 4.0% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2, 6, 24 and 28) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (24) and X (28) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCC(=O)N)C(=O)NCC(=O)NC(CC(C)C)C(=O)NC(C(=O)N2C(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C)CC(C)C)CCCC[NH3+])CCC2)(C)CCCC=CCCC1)CCCC[NH3+])CCC(=O)N)C(CC)C)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])CCC(=O)[O-])CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCNC(=[NH2+])N)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCNC(=[NH2+])N)NC(=O)C(NC(=O)C[NH3+])(C)CCCC=CCCC1)CCCNC(=[NH2+])N)CCCC[NH3+])Cc1ccccc1)CCCNC(=[NH2+])N)CC(=O)N)CCCC[NH3+])C(CC)C
DRAMP21542	GⓍGKFⓍHSKKKFGKAⓍVGEⓍBNS	GXGKFXHSKKKFGKAXVGEXBNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+4)1,15(A9K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 6.25 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.56 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.12 μg/mL)	[Ref.31427820] It has 1.9% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2, 6, 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The B (position: 21) in sequence is norlercine. ③Ⓧ (2) and Ⓧ (6), Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)C)(C)CCCC=CCCC1)C)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C(NC(=O)C(NC(=O)C1(C)NC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(NC(=O)C[NH3+])(C)CCCC=CCCC1)Cc1nc[nH]c1)CO
DRAMP21543	GⓍFSKⓍKGKKIKNLⓍISGⓍKG	GXFSKXKGKKIKNLXISGXKG	GIFSKLAGKKIKNLLISGLK	21	Esc(i+4)1,14(A7K)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 12.5 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.56 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 1.56 μg/mL)	[Ref.31427820] It has 2.5% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2, 6, 15 and 19) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (15) and Ⓧ (19) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(CC)C)C(=O)NC(CO)C(=O)NCC(=O)NC(C(=O)NC(C(=O)NCC=O)CCCC[NH3+])(C)CCCC=CCCC1)CC(C)C)CC(=O)N)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CO)NC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)C[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])CCCC[NH3+])C(CC)C
DRAMP21544	GⓏGKFLHSⓍKKFGKAFVGEIJNS	GZGKFLHSXKKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 10.51 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.42 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.63 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.72 μg/mL)	[Ref.31427820] It has 49.7% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 9) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 2) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (9) and Ⓩ (2) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CO)NC(=O)C(Cc2[nH]cnc2)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(NC(=O)C[NH3+])(C)CCCCCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21545	GIⓏKFLHSAⓍKFGKAFVGEIJNS	GIZKFLHSAXKFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 12.50 μg/mL), Bacillus cereus ATCC 14579 (MIC = 8.84 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 4.42 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 21.02 μg/mL)	[Ref.31427820] It has 66.1% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 10) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 3) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (10) and Ⓩ (3) are cross-linked by hydrocarbon stapling. 	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C)NC(=O)C(CO)NC(=O)C(Cc2[nH]cnc2)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C[NH3+])C(CC)C)(C)CCCCCCC=CCCC1)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21546	GIGⓏFLHSAKⓍFGKAFVGEIJNS	GIGZFLHSAKXFGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 14.87 μg/mL), Bacillus cereus ATCC 14579 (MIC = 12.50 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 10.51 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 21.02 μg/mL)	[Ref.31427820] It has 52.6% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 11) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 4) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (11) and Ⓩ (4) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(C)NC(=O)C(CO)NC(=O)C(Cc2nc[nH]c2)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)(C)CCCCCCC=CCCC1)Cc1ccccc1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21547	GIGKⓏLHSAKKⓍGKAFVGEIJNS	GIGKZLHSAKKXGKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 21.02 μg/mL), Bacillus cereus ATCC 14579 (MIC = 5.26 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.21 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 6.25 μg/mL)	[Ref.31427820] It has 42.5% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 12) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 5) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (12) and Ⓩ (5) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C)NC(=O)C(CO)NC(=O)C(Cc2[nH]cnc2)NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])(C)CCCCCCC=CCCC1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21548	GIGKFⓏHSAKKFⓍKAFVGEIJNS	GIGKFZHSAKKFXKAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)5	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 8.84 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.13 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.13 μg/mL)	[Ref.31427820] It has 82.9% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 13) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 6) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (13) and Ⓩ (6) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C)NC(=O)C(CO)NC(=O)C(Cc2[nH]cnc2)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)(C)CCCCCCC=CCCC1)CCCC[NH3+])C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21549	GIGKFLⓏSAKKFGⓍAFVGEIJNS	GIGKFLZSAKKFGXAFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)6	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 6.25 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.42 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 14.87 μg/mL)	[Ref.31427820] It has 45.3% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 14) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 7) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (14) and Ⓩ (7) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C)NC(=O)C(CO)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)(C)CCCCCCC=CCCC1)C)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21550	GIGKFLHⓏAKKFGKⓍFVGEIJNS	GIGKFLHZAKKFGKXFVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)7	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 3.72 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.72 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 5.26 μg/mL)	[Ref.31427820] It has 95.3% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 15) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 8) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (15) and Ⓩ (8) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)(C)CCCCCCC=CCCC1)Cc1ccccc1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21551	GIGKFLHSⓏKKFGKAⓍVGEIJNS	GIGKFLHSZKKFGKAXVGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)8	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 6.25 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.72 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.21 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.72 μg/mL)	[Ref.31427820] It has 85.2% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 16) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 9) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (16) and Ⓩ (9) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C1(C)NC(=O)C(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)(C)CCCCCCC=CCCC1)C(C)C)CCC(=O)[O-])C(CC)C
DRAMP21552	GIGKFLHSAⓏKFGKAFⓍGEIJNS	GIGKFLHSAZKFGKAFXGEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)9	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 3.72 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.42 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.72 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 5.26 μg/mL)	[Ref.31427820] It has 94.6% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 17) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 10) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (17) and Ⓩ (10) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)CNC(=O)C1(C)NC(=O)C(Cc2ccccc2)NC(=O)C(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(Cc2ccccc2)NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)C)(C)CCCCCCC=CCCC1)CCC(=O)[O-])C(CC)C
DRAMP21553	GIGKFLHSAKⓏFGKAFVⓍEIJNS	GIGKFLHSAKZFGKAFVXEIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)10	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 4.42 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.72 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.13 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 7.43 μg/mL)	[Ref.31427820] It has 43.8% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 18) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 11) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (18) and Ⓩ (11) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2nc[nH]c2)CO)C)CCCC[NH3+])(C)CCCCCCC=CCCC1)CCC(=O)[O-])C(CC)C
DRAMP21554	GIGKFLHSAKKⓏGKAFVGⓍIJNS	GIGKFLHSAKKZGKAFVGXIJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)11	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 2.63 μg/mL), Bacillus cereus ATCC 14579 (MIC = 2.63 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.21 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 2.21 μg/mL)	[Ref.31427820] It has 84.7% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 19) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 12) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (19) and Ⓩ (12) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)C(NC(=O)C1(C)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(Cc2ccccc2)NC(=O)C(C)NC(=O)C(CCCC[NH3+])NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C[NH3+])C(CC)C)CCCC[NH3+])Cc2ccccc2)CC(C)C)Cc2[nH]cnc2)CO)C)CCCC[NH3+])CCCC[NH3+])(C)CCCCCCC=CCCC1)C(CC)C
DRAMP21555	GIGKFLHSAKKFⓏKAFVGEⓍJNS	GIGKFLHSAKKFZKAFVGEXJNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)12	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 7.44 μg/mL), Bacillus cereus ATCC 14579 (MIC = 3.72 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.21 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.13 μg/mL)	[Ref.31427820] It has 75.4% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 20) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 13) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (20) and Ⓩ (13) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(Cc2ccccc2)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)CCCC)(C)CCCC=CCCCCCC1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21556	GIGKFLHSAKKFGⓏAFVGEIⓍNS	GIGKFLHSAKKFGZAFVGEIXNS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)13	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 7.44 μg/mL), Bacillus cereus ATCC 14579 (MIC = 4.42 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.21 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 6.25 μg/mL)	[Ref.31427820] It has 63.5% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 21) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 14) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③Ⓧ (21) and Ⓩ (14) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC1(C)C(=O)NC(C)C(=O)NC(Cc2ccccc2)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(CC)C)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CO)CC(=O)N)(C)CCCC=CCCCCCC1)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21557	GIGKFLHSAKKFGKⓏFVGEIJⓍS	GIGKFLHSAKKFGKZFVGEIJXS	GIGKFLHSAKKFGKAFVGEIMNS	23	Mag(i+7)14	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in potassium phosphate buffer.	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.31427820] Gram-positive bacteria: Staphyolococcus aureus ATCC 25923 (MIC = 2.63 μg/mL), Bacillus cereus ATCC 14579 (MIC = 1.56 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 1.86 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 5.26 μg/mL)	[Ref.31427820] It has 68.1% hemolysis against human red blood cells at 25 μg/mL.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 22) in sequence is S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓩ (position: 15) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ③The J (position: 21) in sequence is norlercine. ④Ⓧ (22) and Ⓩ (15) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference	31427820	Nat Biotechnol. 2019 Oct;37(10):1186-1197. doi: 10.1038/s41587-019-0222-z. Epub 2019 Aug 19.	Rida Mourtada, Henry D Herce, Daniel J Yin, Jamie A Moroco, Thomas E Wales, John R Engen, Loren D Walensky	Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice	Stapled AMP						O=C(NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC1(C)C(=O)NC(Cc2ccccc2)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CCC(=O)[O-])C(=O)NC(C(CC)C)C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CO)(C)CCCC=CCCCCCC1)CCCC[NH3+])Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C)CO)Cc1[nH]cnc1)CC(C)C)Cc1ccccc1)CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP21558	KⓍWKJⓍK	KXWKJXK	/	7	KKK	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	①[Ref.30361948] All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices. ②[Ref.28547390] Peptide NLE and LYS maintained a compatible helicity to LEU.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphyolococcus aureus ATCC 6538p (MIC = 6.3 μM),  Staphylococcus epidermidis ATCC 12228 (MIC= 25 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysenteriae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 18.8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM).##[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 6.3 μg/mL), Staphylococcus aureus (MIC = 6.3 μg/mL), Staphylococcus epidermidis (MIC = 12.5 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 12.5 μg/mL), Shigella dysenteriae (MIC = 12.5 μg/mL), Salmonella typhimurium (MIC = 50 μg/mL), Klebsiella pneumoniae (MIC = 18.8 μg/mL), Pseudomonas aeruginosa (MIC = 12.5 μg/mL).	[Ref.30361948] It has 1.5% hemolysis against human red blood cells at 25 μM and 3.0% hemolysis at 50 μM.##[Ref.28547390] 3.3% hemolysis against human red blood cells at 25 μM and 7.9% hemolysis t 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948##28547390	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.##Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim. ##Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides.##Mono-substitution effects on antimicrobial activity of stapled heptapeptides.	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21559	RⓍWKJⓍK	RXWKJXK	/	7	RKK	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 6.3 μM), Staphyolococcus aureus ATCC 6538p (MIC = 6.3 μM),  Staphylococcus epidermidis ATCC 12228 (MIC= 12.5 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysenteriae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 25 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 12.5 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM)	[Ref.30361948] It has 1.5% hemolysis against human red blood cells at 25 μM and 4.3% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCNC(=[NH2+])N
DRAMP21560	KⓍWRJⓍK	KXWRJXK	/	7	KRK	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphyolococcus aureus ATCC 6538p (MIC = 6.3 μM),  Staphylococcus epidermidis ATCC 12228 (MIC= 25 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysenteriae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC = 75 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 37.5 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM)	[Ref.30361948] It has <1% hemolysis against human red blood cells at 25 μM and 2.0% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21561	KⓍWKJⓍR	KXWKJXR	/	7	KKR	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 9.4 μM), Staphyolococcus aureus ATCC 6538p (MIC = 6.3 μM),  Staphylococcus epidermidis ATCC 12228 (MIC = 25 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysenteriae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 12.5 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM)	[Ref.30361948] It has 1.4% hemolysis against human red blood cells at 25 μM and % hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21562	RⓍWRJⓍK	RXWRJXK	/	7	RRK	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphyolococcus aureus ATCC 6538p (MIC = 6.3 μM),  Staphylococcus epidermidis ATCC 12228 (MIC = 25 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysenteriae ATCC 9752 (MIC = 37.5 μM), Salmonella typhimurium ATCC 14028 (MIC = 100 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 50 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 37.5 μM)	[Ref.30361948] It has <1% hemolysis against human red blood cells at 25 μM and <1% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCNC(=[NH2+])N
DRAMP21563	RⓍWKJⓍR	RXWKJXR	/	7	RKR	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 6.3 μM), Staphyolococcus aureus ATCC 6538p (MIC = 3.2 μM),  Staphylococcus epidermidis ATCC 12228 (MIC = 12.5 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 6.3 μM), Shigella dysenteriae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 25 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 18.8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM)	[Ref.30361948] It has 8.2% hemolysis against human red blood cells at 25 μM and 17.0% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C([NH3+])CCCNC(=[NH2+])N
DRAMP21564	KⓍWRJⓍR	KXWRJXR	/	7	KRR	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 6.3 μM), Staphyolococcus aureus ATCC 6538p (MIC = 3.2 μM),  Staphylococcus epidermidis ATCC 12228 (MIC = 12.5 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysenteriae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 18.8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 37.5 μM)	[Ref.30361948] It has 1.8% hemolysis against human red blood cells at 25 μM and 5.6% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21565	RⓍWRJⓍR	RXWRJXR	/	7	RRR	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate solution (pH 6.5).	All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphyolococcus aureus ATCC 6538p (MIC = 6.3 μM),  Staphylococcus epidermidis ATCC 12228 (MIC = 25 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysenteriae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC = 100 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 50 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 100 μM)	[Ref.30361948] It has <1% hemolysis against human red blood cells at 25 μM and 3.2% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The J (position: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30361948	Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(CCCC)C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C([NH3+])CCCNC(=[NH2+])N
DRAMP21566	IDWKKⓍLDAⓍKQIL	IDWKKXLDAXKQIL	IDWKKLLDAAKQIL	14	MP1S	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		96.1% α-helical content in a 25 mM potassium phosphate buffer solution at 20℃	①Helical contents of all stapled analogues were increased by more than a three-fold compared to their unmodified counterpart, MP1. ②MP1S appears to be the most helical among this panel of peptides, showing 96% helicity, which is 3.7-fold higher than that of MP1.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.29075946] Gram-positive bacteria: Bacillus subtilis (MIC = 1.6 μg/mL), Staphylococcus aureus (MIC = 2.4 μg/mL), Staphylococcus epidermidis (MIC > 100 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC > 100 μg/mL), Shigella dysenteriae (MIC > 100 μg/mL), Salmonella typhimurium (MIC > 100 μg/mL), Klebsiella pneumoniae (MIC > 100 μg/mL), Pseudomonas aeruginosa (MIC > 100 μg/mL)	[Ref.29075946] It has 6.7% hemolysis against human red blood cells at 12.5 μM and 12.3% hemolysis at 25 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	29075946	Arch Pharm Res. 2017 Dec;40(12):1414-1419. doi: 10.1007/s12272-017-0963-5. Epub 2017 Oct 26.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim 	Antimicrobial activity and stability of stapled helices of polybia-MP1	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CC(=O)[O-])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CC(C)C)C(CC)C)CCC(=O)N)CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])Cc1c2c([nH]c1)cccc2)CC(=O)[O-])C([NH3+])C(CC)C
DRAMP21567	IDWKKⓍLNAⓍKQIL	IDWKKXLNAXKQIL	IDWKKLLDAAKQIL	14	MP1S-D8N	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		89.4% α-helical content in a 25 mM potassium phosphate buffer solution at 20℃	①Helical contents of all stapled analogues were increased by more than a three-fold compared to their unmodified counterpart, MP1. ②MP1S-D8N and MP1S-Q12K showed slightly lower helical contents (89.4% and 81.8, respectively).	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.29075946] Gram-positive bacteria: Bacillus subtilis (MIC = 0.8 μg/mL), Staphylococcus aureus (MIC = 0.8 μg/mL), Staphylococcus epidermidis (MIC = 37.5 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 50 μg/mL), Shigella dysenteriae (MIC = 100 μg/mL), Salmonella typhimurium (MIC > 100 μg/mL), Klebsiella pneumoniae (MIC = 37.5 μg/mL), Pseudomonas aeruginosa (MIC ≥ 100 μg/mL)	[Ref.29075946] It has 16.3% hemolysis against human red blood cells at 12.5 μM and 37.8% hemolysis at 25 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	29075946	Arch Pharm Res. 2017 Dec;40(12):1414-1419. doi: 10.1007/s12272-017-0963-5. Epub 2017 Oct 26.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim 	Antimicrobial activity and stability of stapled helices of polybia-MP1	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CC(=O)N)C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CC(C)C)C(CC)C)CCC(=O)N)CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])Cc1c2c([nH]c1)cccc2)CC(=O)[O-])C([NH3+])C(CC)C
DRAMP21568	IDWKKⓍLDAⓍKKIL	IDWKKXLDAXKKIL	IDWKKLLDAAKQIL	14	MP1S-Q12K	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		81.8% α-helical content in a 25 mM potassium phosphate buffer solution at 20℃	①Helical contents of all stapled analogues were increased by more than a three-fold compared to their unmodified counterpart, MP1. ②MP1S-D8N and MP1S-Q12K showed slightly lower helical contents (89.4% and 81.8, respectively).	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.29075946] Gram-positive bacteria: Bacillus subtilis (MIC = 0.8 μg/mL), Staphylococcus aureus (MIC = 1.2 μg/mL), Staphylococcus epidermidis (MIC = 50 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC >100  μg/mL), Shigella dysenteriae (MIC > 100 μg/mL), Salmonella typhimurium (MIC > 100 μg/mL), Klebsiella pneumoniae (MIC > 100 μg/mL), Pseudomonas aeruginosa (MIC > 100 μg/mL)	[Ref.29075946] It has 9.6% hemolysis against human red blood cells at 12.5 μM and 13.9% hemolysis at 25 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	29075946	Arch Pharm Res. 2017 Dec;40(12):1414-1419. doi: 10.1007/s12272-017-0963-5. Epub 2017 Oct 26.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim 	Antimicrobial activity and stability of stapled helices of polybia-MP1	Stapled AMP						O=C([NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C)NC(=O)C(CC(=O)[O-])NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CC(=O)[O-])Cc2c3c([nH]c2)cccc3)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])C(CC)C)CC(C)C
DRAMP21569	KⓍWKAⓍK	KXWKAXK	/	7	ALA	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 25 μg/mL), Staphylococcus aureus (MIC = 25 μg/mL), Staphylococcus epidermidis (MIC = 100 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 25 μg/mL), Shigella dysenteriae (MIC = 50 μg/mL), Salmonella typhimurium (MIC = 100 μg/mL), Klebsiella pneumoniae (MIC = 25 μg/mL), Pseudomonas aeruginosa (MIC = 25 μg/mL)	[Ref.28547390] It has <1% hemolysis against human red blood cells at 25 μM and <1% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21570	KⓍWKLⓍK	KXWKLXK	/	7	LEU	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 25 μg/mL), Staphylococcus aureus (MIC = 12.5 μg/mL), Staphylococcus epidermidis (MIC = 50 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 12.5 μg/mL), Shigella dysenteriae (MIC = 25 μg/mL), Salmonella typhimurium (MIC = 50 μg/mL), Klebsiella pneumoniae (MIC = 18.8 μg/mL), Pseudomonas aeruginosa (MIC = 18.8 μg/mL)	[Ref.28547390] It has <1% hemolysis against human red blood cells at 25 μM and <1% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21571	KⓍWKVⓍK	KXWKVXK	/	7	VAL	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	Compared to LEU, the previously reported stapled heptapeptide containing leucine in position 5, peptides VAL and ILE, carrying valine and isoleucine, respectively, appeared slightly more helical as determined by the CD signal intensity at 222 nm.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 18.8 μg/mL), Staphylococcus aureus (MIC = 12.5 μg/mL), Staphylococcus epidermidis (MIC = 50 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 18.8 μg/mL), Shigella dysenteriae (MIC = 25 μg/mL), Salmonella typhimurium (MIC = 100 μg/mL), Klebsiella pneumoniae (MIC = 18.8 μg/mL), Pseudomonas aeruginosa (MIC = 12.5 μg/mL)	[Ref.28547390] It has 1.3% hemolysis against human red blood cells at 25 μM and 2.5% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21572	KⓍWKIⓍK	KXWKIXK	/	7	ILE	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	Compared to LEU, the previously reported stapled heptapeptide containing leucine in position 5, peptides VAL and ILE, carrying valine and isoleucine, respectively, appeared slightly more helical as determined by the CD signal intensity at 222 nm.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 25 μg/mL), Staphylococcus aureus (MIC = 25 μg/mL), Staphylococcus epidermidis (MIC = 50 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 25 μg/mL), Shigella dysenteriae (MIC = 25 μg/mL), Salmonella typhimurium (MIC = 100 μg/mL), Klebsiella pneumoniae (MIC = 37.5 μg/mL), Pseudomonas aeruginosa (MIC = 12.5 μg/mL)	[Ref.28547390] It has 1.5% hemolysis against human red blood cells at 25 μM and 3.0% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(C(CC)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21573	KⓍWKFⓍK	KXWKFXK	/	7	PHE	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	On the other hand, peptide PHE, TRP, and GLU, bearing phenylalanine, tryptophan, and glutamate, respectively, showed a slightly decreased helicity.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 25 μg/mL), Staphylococcus aureus (MIC = 25 μg/mL), Staphylococcus epidermidis (MIC = 50 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 25 μg/mL), Shigella dysenteriae (MIC = 50 μg/mL), Salmonella typhimurium (MIC = 100 μg/mL), Klebsiella pneumoniae (MIC = 25 μg/mL), Pseudomonas aeruginosa (MIC = 12.5 μg/mL)	[Ref.28547390] It has 1.9% hemolysis against human red blood cells at 25 μM and 4.4% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2ccccc2)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21574	KⓍWKWⓍK	KXWKWXK	/	7	TRP	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	On the other hand, peptide PHE, TRP, and GLU, bearing phenylalanine, tryptophan, and glutamate, respectively, showed a slightly decreased helicity.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 12.5 μg/mL), Staphylococcus aureus (MIC = 12.5 μg/mL), Staphylococcus epidermidis (MIC = 25 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 12.5 μg/mL), Shigella dysenteriae (MIC = 25 μg/mL), Salmonella typhimurium (MIC = 50 μg/mL), Klebsiella pneumoniae (MIC = 12.5 μg/mL), Pseudomonas aeruginosa (MIC = 12.5 μg/mL)	[Ref.28547390] It has 3.2% hemolysis against human red blood cells at 25 μM and 5.9% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21575	KⓍWKEⓍK	KXWKEXK	/	7	GLU	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	On the other hand, peptide PHE, TRP, and GLU, bearing phenylalanine, tryptophan, and glutamate, respectively, showed a slightly decreased helicity.	Not found	Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 100 μg/mL.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC > 100 μg/mL), Staphylococcus aureus (MIC > 100 μg/mL), Staphylococcus epidermidis (MIC > 100 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 37.5 μg/mL), Shigella dysenteriae (MIC > 100 μg/mL), Salmonella typhimurium (MIC > 100 μg/mL), Klebsiella pneumoniae (MIC = 50 μg/mL), Pseudomonas aeruginosa (MIC = 25 μg/mL)	[Ref.28547390] It has <1% hemolysis against human red blood cells at 25 μM and <1% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCC(=O)[O-])C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21576	KⓍWKKⓍK	KXWKKXK	/	7	LYS	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	Peptide NLE and LYS maintained a compatible helicity to LEU.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 100 μg/mL), Staphylococcus aureus (MIC = 50 μg/mL), Staphylococcus epidermidis (MIC > 100 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 50 μg/mL), Shigella dysenteriae (MIC = 100 μg/mL), Salmonella typhimurium (MIC > 100 μg/mL), Klebsiella pneumoniae (MIC = 75 μg/mL), Pseudomonas aeruginosa (MIC = 6.3 μg/mL)	[Ref.28547390] It has <1% hemolysis against human red blood cells at 25 μM and <1% hemolysis at 50 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28547390	Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.	Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim	Mono-substitution effects on antimicrobial activity of stapled heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21578	WWVⓍARAⓍRR	WWVXARAXRR	WWVXARAXRR	10	Val-HSLP	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		0.0% α-helix and 34.3% β-strand in 20 mM potassium phosphate buffer; 0.8% α-helix and 36.9% β-strand in 20 mM potassium phosphate buffer made 30% in TFE.	Only slghtly higher β-strand characteristics were observed for the hydrocarbon-stapled peptides in 30% TFE. Overall, the peptides showed some β-strand secondary structural characteristics and little α-helical content.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 20 μM.	[Ref.28073163] Gram-positive bacteria: Bacillus megaterium ATCC 14581 (IC50 = 0.69 μM, MIC = 5.00 μM), Staphylococcus aureus ATCC 6538 (IC50 = 0.63 μM, MIC = 5.00 μM), Enterococcus faecalis ATCC 29212 (IC50 = 0.65 μM, MIC = 5.00 μM);##Gram-negative bacteria: Escherichia coli ATCC 700926 (IC50 = 14.8 μM, MIC > 20 μM);## Fungi: Candida albicans 002 ATCC 64385 (IC50 > 20 μM, MIC > 20 μM), C. albicans 004 ATCC MYA-2876 (IC50 > 20 μM, MIC > 20 μM).	[Ref.28073163] HC50 = 14.5 μM against human red blood cells. Note:  HC50 is the half-maximal hemolytic concentration.	Cyclic (Stapled)	Acylation (Valerylamide)	Amidation	①The Ⓧ (position: 4 and 8) in sequence indicates (S)-2-(4'-pentenyl)-alanine. ②Ⓧ (4) and Ⓧ (8) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28073163	Biopolymers. 2017 May;108(3). doi: 10.1002/bip.23006.	Zachary B Jenner, Christopher M Crittenden, Martín Gonzalez, Jennifer S Brodbelt, Kerry A Bruns	Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C(NC(=O)C(NC(=O)C(NC(=O)C)Cc1c2c([nH]c1)cccc2)Cc1c2c([nH]c1)cccc2)C(C)C.CC.[H+H0].[H+H0].[H+H0]
DRAMP21580	WWVⓍAFAⓍRRR	WWVXAFAXRRR	WWVXAFAXRRR	11	Cap-HSLP	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		0.3% α-helix and 31.9% β-strand in 20 mM potassium phosphate buffer; 0.7% α-helix and 40.0% β-strand in 20 mM potassium phosphate buffer made 30% in TFE.	Only slghtly higher β-strand characteristics were observed for the hydrocarbon-stapled peptides in 30% TFE. Overall, the peptides showed some β-strand secondary structural characteristics and little α-helical content.	Not found	Function: Antibacterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria and antifungal activity against Candida albicans are not noteable under 20 μM.	[Ref.28073163] Gram-positive bacteria: Bacillus megaterium ATCC 14581 (IC50 = 1.63 μM, MIC = 5.00 μM), Staphylococcus aureus ATCC 6538 (IC50 = 0.64 μM, MIC = 5.00 μM), Enterococcus faecalis ATCC 29212 (IC50 = 0.63 μM, MIC = 1.25 μM);##Gram-negative bacteria: Escherichia coli ATCC 700926 (IC50 = 169 μM, MIC > 20 μM);## Fungi: Candida albicans 002 ATCC 64385 (IC50 > 20 μM, MIC > 20 μM), C. albicans 004 ATCC MYA-2876 (IC50 > 20 μM, MIC > 20 μM).	[Ref.28073163] HC50 = 4.49 μM against human red blood cells. Note:  HC50 is the half-maximal hemolytic concentration.	Cyclic (Stapled)	Acylation (Caproylamide)	Amidation	①The Ⓧ (position: 4 and 8) in sequence indicates (S)-2-(4'-pentenyl)-alanine. ②Ⓧ (4) and Ⓧ (8) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	28073163	Biopolymers. 2017 May;108(3). doi: 10.1002/bip.23006.	Zachary B Jenner, Christopher M Crittenden, Martín Gonzalez, Jennifer S Brodbelt, Kerry A Bruns	Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(Cc2ccccc2)C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C(NC(=O)C(NC(=O)C(NC(=O)C)Cc1c2c([nH]c1)cccc2)Cc1c2c([nH]c1)cccc2)C(C)C.C(C)C.[H+H0].[H+H0].[H+H0]
DRAMP21582	KⓍWKLⓍK	KXWKLXK	/	7	S3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		Stable α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. 	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μg/mL), Staphylcocccus aureus ATCC 6538p (MIC = 25 μg/mL), Staphylcococcus epidermis ATCC 12228 (MIC = 100 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μg/mL), Shigella dysentariae ATCC 9752 (MIC = 50 μg/mL), Salmonella typhimurium ATCC 14028 (MIC = 100 μg/mL), Klebsiella pneumonia ATCC 10031 (MIC = 50 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 75 μg/mL)	It has <1% hemolysis against human red blood cells at 6.3 μM and <1% hemolysis at 12.5 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2016 Aug;37(8)1199-1203. doi: 10.1002/bkcs.10839.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21583	KⓍWKLⓍKGKⓍWKLⓍK	KXWKLXKGKXWKLXK	/	15	3GL3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	3GL3 apperaed to be the most helical in this series as indicated by the distinct double minima near at 208 and 222 nm with similar intensities.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. 	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 2.3 μg/mL), Staphylcocccus aureus ATCC 6538p (MIC = 1.6 μg/mL), Staphylcococcus epidermis ATCC 12228 (MIC = 3.1 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.1 μg/mL), Shigella dysentariae ATCC 9752 (MIC = 37.5 μg/mL), Salmonella typhimurium ATCC 14028 (MIC = 50 μg/mL), Klebsiella pneumonia ATCC 10031 (MIC = 6.3 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 9.4 μg/mL)	It has 19.1% hemolysis against human red blood cells at 6.3 μM and 31.8% hemolysis at 12.5 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2, 6, 10 and 14) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (10) and Ⓧ (14) are cross-linked respectively by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2016 Aug;37(8)1199-1203. doi: 10.1002/bkcs.10839.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC2(C)C(=O)NC(Cc3c4c([nH]c3)cccc4)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC2)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21584	KⓍWKLⓍKAKⓍWKLⓍK	KXWKLXKAKXWKLXK	/	15	3BA3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. 	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 2.3 μg/mL), Staphylcocccus aureus ATCC 6538p (MIC = 1.6 μg/mL), Staphylcococcus epidermis ATCC 12228 (MIC = 3.1 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.1 μg/mL), Shigella dysentariae ATCC 9752 (MIC = 6.3 μg/mL), Salmonella typhimurium ATCC 14028 (MIC = 12.5 μg/mL), Klebsiella pneumonia ATCC 10031 (MIC = 3.1 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 3.1 μg/mL)	It has 14.2% hemolysis against human red blood cells at 6.3 μM and 24.9% hemolysis at 12.5 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The A (position: 8) in sequence is β-Ala. ②The Ⓧ (position: 2, 6, 10 and 14) in sequence indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6), Ⓧ (10) and Ⓧ (14) are cross-linked respectively by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2016 Aug;37(8)1199-1203. doi: 10.1002/bkcs.10839.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2(C)C(=O)NC(Cc3c4c([nH]c3)cccc4)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC2)CCCC[NH3+])C)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21585	KⓍWKLⓍKBKⓍWKLⓍK	KXWKLXKBKXWKLXK	/	15	3GA3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. 	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 4.0 μg/mL), Staphylcocccus aureus ATCC 6538p (MIC = 3.1 μg/mL), Staphylcococcus epidermis ATCC 12228 (MIC = 12.5 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 4.7 μg/mL), Shigella dysentariae ATCC 9752 (MIC = 18.8 μg/mL), Salmonella typhimurium ATCC 14028 (MIC = 37.5 μg/mL), Klebsiella pneumonia ATCC 10031 (MIC = 9.4 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 9.4 μg/mL)	It has 12.9% hemolysis against human red blood cells at 6.3 μM and 24.4% hemolysis at 12.5 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The B (position: 8) in sequence is γ-aminobutyric acid (GABA). ②The Ⓧ (position: 2, 6, 10 and 14) in sequence indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6), Ⓧ (10) and Ⓧ (14) are cross-linked respectively by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2016 Aug;37(8)1199-1203. doi: 10.1002/bkcs.10839.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C(=O)NCCCC(=O)NC(C(=O)NC2(C)C(=O)NC(Cc3c4c([nH]c3)cccc4)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C(=O)[NH-])CCCC[NH3+])(C)CCCC=CCCC2)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21586	KⓍWKLⓍKPKⓍWKLⓍK	KXWKLXKPKXWKLXK	/	15	3PR3-X	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	"Whereas all other
dimeric analogs were obtained as a single exclusive product,
the proline-containing sequence yielded two products
(3PR3-X and 3PR3-Y) in similar amounts. These might be
conformational isomers induced by the cis–trans configuration
of the proline linker. 3PR3-X, which showed the weakest hemolytic activity, displayed a CD spectrum similar to that of the monomeric S3 and the lowest helical content in this series."	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. 	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 3.1 μg/mL), Staphylcocccus aureus ATCC 6538p (MIC = 4.7 μg/mL), Staphylcococcus epidermis ATCC 12228 (MIC = 12.5 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.1 μg/mL), Shigella dysentariae ATCC 9752 (MIC = 6.3 μg/mL), Salmonella typhimurium ATCC 14028 (MIC = 12.5 μg/mL), Klebsiella pneumonia ATCC 10031 (MIC = 4.7 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 9.4 μg/mL)	It has 5.7% hemolysis against human red blood cells at 6.3 μM and 9.7% hemolysis at 12.5 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2, 6, 10 and 14) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (10) and Ⓧ (14) are cross-linked respectively by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple. 	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2016 Aug;37(8)1199-1203. doi: 10.1002/bkcs.10839.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C(=O)N2C(C(=O)NC(C(=O)NC3(C)C(=O)NC(Cc4c5c([nH]c4)cccc5)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC3)CCCC[NH3+])CCC2)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21587	KⓍWKLⓍKPKⓍWKLⓍK	KXWKLXKPKXWKLXK	/	15	3PR3-Y	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution at 20 ℃	"Whereas all other
dimeric analogs were obtained as a single exclusive product,
the proline-containing sequence yielded two products
(3PR3-X and 3PR3-Y) in similar amounts. These might be
conformational isomers induced by the cis–trans configuration
of the proline linker."	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 1.2 μg/mL), Staphylcocccus aureus ATCC 6538p (MIC = 1.2 μg/mL), Staphylcococcus epidermis ATCC 12228 (MIC = 4.7 μg/mL);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 2.3 μg/mL), Shigella dysentariae ATCC 9752 (MIC = 4.7 μg/mL), Salmonella typhimurium ATCC 14028 (MIC = 12.5 μg/mL), Klebsiella pneumonia ATCC 10031 (MIC = 3.1 μg/mL), Pseudomonas aeruginosa ATCC 27853 (MIC = 6.3 μg/mL)	It has 16.2% hemolysis against human red blood cells at 6.3 μM and 31.9% hemolysis at 12.5 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2, 6, 10 and 14) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (10) and Ⓧ (14) are cross-linked respectively by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple. ③The P (position: 8) in sequence is D-proline.	Mixed (D-Pro8)	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2016 Aug;37(8)1199-1203. doi: 10.1002/bkcs.10839.	Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers	Stapled AMP						
DRAMP21588	KⓍWKAⓍK	KXWKAXK	/	7	Ac-S1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution (pH 6.5)	On the contraty, conformations of sequences S1 and S3 appear to be not greatly affected by the presence of the N-acetyl cap.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 25 μM), Staphylcocccus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 37.5 μM), Shigella dysentariae ATCC 9752 (MIC = 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 50 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 50 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0% and <1.0% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21589	KⓍWKAⓍK	KXWKAXK	/	7	H-S1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution (pH 6.5)	On the contraty, conformations of sequences S1 and S3 appear to be not greatly affected by the presence of the N-acetyl cap.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 37.5 μM), Staphylcocccus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 100 μM), Salmonella typhimurium ATCC 14028 (MIC = 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 25 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 25 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0% and <1.0% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						
DRAMP21590	KⓍAKWⓍK	KXAKWXK	/	7	Ac-S2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution (pH 6.5)	Conformational analysis using far ultraviolet CD spectrometry indicates that the removal of the N-acetyl cap from Ac-S2 and Ac-S4 causes a significant loss of their helical contents.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 37.5 μM), Staphylcocccus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 37.5 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 50 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0% and <1.0% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21591	KⓍAKWⓍK	KXAKWXK	/	7	H-S2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix (but less helical than Ac-S2) in a 25 mM potassium phosphate buffer solution (pH 6.5)	Conformational analysis using far ultraviolet CD spectrometry indicates that the removal of the N-acetyl cap from Ac-S2 and Ac-S4 causes a significant loss of their helical contents.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 37.5 μM), Staphylococcus aureus ATCC 6538p (MIC = 37.5 μM), Staphylcocccus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 50 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 50 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 37.5 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0% and <1.0% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						
DRAMP21592	KⓍWKLⓍK	KXWKLXK	/	7	Ac-S3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution (pH 6.5)	On the contraty, conformations of sequences S1 and S3 appear to be not greatly affected by the presence of the N-acetyl cap.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 18.8 μM), Staphylococcus aureus ATCC 6538p (MIC = 25 μM), Staphylcocccus epidermis ATCC 12228 (MIC = 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC = 75 μM), Klebsiella pneumonia ATCC 10031 (MIC = 37.5 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 50 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, 1.59% and 5.53% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21593	KⓍWKLⓍK	KXWKLXK	/	7	H-S3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution (pH 6.5)	①On the contraty, conformations of sequences S1 and S3 appear to be not greatly affected by the presence of the N-acetyl cap. ②It should be also noted that H-S3 displays a CD spectrum that is typically observed from α-helical peptides even without the N-acetyl cal.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphylococcus aureus ATCC 6538p (MIC = 12.5 μM), Staphylcocccus epidermis ATCC 12228 (MIC = 25 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysentariae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumonia ATCC 10031 (MIC = 25 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 25 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0% and 2.05% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						
DRAMP21594	KⓍLKWⓍK	KXLKWXK	/	7	Ac-S4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in a 25 mM potassium phosphate buffer solution (pH 6.5)	Conformational analysis using far ultraviolet CD spectrometry indicates that the removal of the N-acetyl cap from Ac-S2 and Ac-S4 causes a significant loss of their helical contents.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphylococcus aureus ATCC 6538p (MIC = 25 μM), Staphylcocccus epidermis ATCC 12228 (MIC = 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC = 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 37.5 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 50 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, 1.29%, 2.84% and 5.74% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						O=C(NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21595	KⓍLKWⓍK	KXLKWXK	/	7	H-S4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix (but less helix content Ac-S4) in a 25 mM potassium phosphate buffer solution (pH 6.5)	Conformational analysis using far ultraviolet CD spectrometry indicates that the removal of the N-acetyl cap from Ac-S2 and Ac-S4 causes a significant loss of their helical contents.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 50 μM), Staphylcocccus epidermis ATCC 12228 (MIC = 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 75 μM), Salmonella typhimurium ATCC 14028 (MIC = 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 37.5 μM), Pseudomonas aeruginose ATCC 27853 (MIC = 25 μM)	It has <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0%, <1.0% and <1.0% hemolysis against human red blood cells at 0.8,1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pententylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC. 2015 Oct;36(10)2511-2515. doi: 10.1002/bkcs.10483.	Thuy T.T. Dinh, Do-Hee Kim, Thang Q. Nguyen, Bong-Jin Lee, Young-Woo Kim	N-Capping Effects of Stapled Heptapeptides on Antimicrobial and Hemolytic Activities	Stapled AMP						
DRAMP21597	KⓍAKAⓍKKAAKAAWK	KXAKAXKKAAKAAWK	KAAKAAKKAAKAAWK	15	Ac-SS-14W	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH6.5)	On the other hand, singly-stapled analog Ac-SS-14W exhibited a typical CD spectrum for α-helix, characterized by two minima near 208 and 222 nm and a maximum near 190 nm. 	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 9.4 μM), Staphylococcus epidermis ATCC 12228 (MIC = 75 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.1 μM), Shigella dysentariae ATCC 9752 (MIC = 18.8 μM), Salmonella typhimurium ATCC 14028 (MIC > 200 μM), Klebsiella pneumonia ATCC 10031 (MIC = 18.8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 100 μM).	[Ref.26235946] It has <1% hemolysis against human red blood cells at 12.5 μM and <1% hemolysis at 25 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	26235946	Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19.	Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim	Antimicrobial activity of doubly-stapled alanine/lysine-based peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc2c3c([nH]c2)cccc3)C)C)CCCC[NH3+])C)C)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21598	KⓍAKAⓍKKⓍAKAⓍWK	KXAKAXKKXAKAXWK	KAAKAAKKAAKAAWK	15	Ac-DS-14W	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH6.5)	Doubly-stapled Ac-Ds-14W showed the most enhaced helical contents among this series of peptides. 	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 1.6 μM), Staphylococcus aureus ATCC 6538p (MIC = 4.8 μM), Staphylococcus epidermis ATCC 12228 (MIC = 3.1 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 200 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 100 μM).	[Ref.26235946] It has 22.1% hemolysis against human red blood cells at 12.5 μM and 38.8% hemolysis at 25 μM. 	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 ,6, 9 and 13) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	26235946	Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19.	Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim	Antimicrobial activity of doubly-stapled alanine/lysine-based peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc3c4c([nH]c3)cccc4)(C)CCCC=CCCC2)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21599	KⓍAKAⓍKKⓍAKWⓍAK	KXAKAXKKXAKWXAK	KAAKAAKKAAKAAWK	15	Ac-DS-12W	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	In addition, the positional modification of tryptophan caused significant changes in the conformation: in the CD analysis, the most active Ac-DS-5W exhibited markedly enhanced helical content whereas the equipotent Ac-DS-12W showed decreased helicity compared to Ac-DS-14W	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 1.6 μM), Staphylococcus aureus ATCC 6538p (MIC = 3.1 μM), Staphylococcus epidermis ATCC 12228 (MIC = 4.8 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 50 μM), Shigella dysentariae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC = 200 μM), Klebsiella pneumonia ATCC 10031 (MIC = 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 100 μM).	[Ref.26235946] It has 25.3% hemolysis against human red blood cells at 12.5 μM and 42.5% hemolysis at 25 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 ,6, 9 and 13) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	26235946	Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19.	Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim	Antimicrobial activity of doubly-stapled alanine/lysine-based peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(Cc3c4c([nH]c3)cccc4)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C)(C)CCCC=CCCC2)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21600	KⓍAKWⓍKKⓍAKAⓍAK	KXAKWXKKXAKAXAK	KAAKAAKKAAKAAWK	15	Ac-DS-3W	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	No other descriptive information about the structure found in the literature	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 3.1 μM), Staphylococcus aureus ATCC 6538p (MIC = 4.8 μM), Staphylococcus epidermis ATCC 12228 (MIC = 4.8 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC = 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 200 μM).	[Ref.26235946] It has 28.9% hemolysis against human red blood cells at 12.5 μM and 42.5% hemolysis at 25 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 ,6, 9 and 13) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	26235946	Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19.	Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim	Antimicrobial activity of doubly-stapled alanine/lysine-based peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C)(C)CCCC=CCCC2)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21601	KⓍWKAⓍKKⓍAKAⓍAK	KXWKAXKKXAKAXAK	KAAKAAKKAAKAAWK	15	Ac-DS-5W	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	In addition, the positional modification of tryptophan caused significant changes in the conformation: in the CD analysis, the most active Ac-DS-5W exhibited markedly enhanced helical content whereas the equipotent Ac-DS-12W showed decreased helicity compared to Ac-DS-14W	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 1.6 μM), Staphylococcus aureus ATCC 6538p (MIC = 1.6 μM), Staphylococcus epidermis ATCC 12228 (MIC = 1.6 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 18.8 μM), Shigella dysentariae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 37.5 μM), Klebsiella pneumonia ATCC 10031 (MIC = 37.5 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM).	[Ref.26235946] It has 22.0% hemolysis against human red blood cells at 12.5 μM and 38.5% hemolysis at 25 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 ,6, 9 and 13) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	26235946	Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19.	Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim	Antimicrobial activity of doubly-stapled alanine/lysine-based peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC2(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C)(C)CCCC=CCCC2)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21602	KⓍAKWⓍKKⓍAKAⓍAK	KXAKWXKKXAKAXAK	KAAKAAKKAAKAAWK	15	Su-DS-5W	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	In the CD experiments, these new analogs showed similar helicity to Ac-DS-5W although Su-DS-5W displayed a slight increase in helicity whereas H-DS-5W exhibited a slight decrease.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 1.6 μM), Staphylococcus aureus ATCC 6538p (MIC = 1.6 μM), Staphylococcus epidermis ATCC 12228 (MIC = 1.6 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysentariae ATCC 9752 (MIC = 50 μM), Salmonella typhimurium ATCC 14028 (MIC > 200 μM), Klebsiella pneumonia ATCC 10031 (MIC = 25 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 50 μM).	[Ref.26235946] It has 19.5% hemolysis against human red blood cells at 12.5 μM and 32.6% hemolysis at 25 μM.	Cyclic (Stapled)	Succinylation	Amidation	①The Ⓧ (position: 2 ,6, 9 and 13) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	26235946	Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19.	Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim	Antimicrobial activity of doubly-stapled alanine/lysine-based peptides	Stapled AMP						
DRAMP21603	KⓍAKWⓍKKⓍAKAⓍAK	KXAKWXKKXAKAXAK	KAAKAAKKAAKAAWK	15	H-DS-5W	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	In the CD experiments, these new analogs showed similar helicity to Ac-DS-5W although Su-DS-5W displayed a slight increase in helicity whereas H-DS-5W exhibited a slight decrease.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.26235946] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 1.6 μM), Staphylococcus aureus ATCC 6538p (MIC = 1.6 μM), Staphylococcus epidermis ATCC 12228 (MIC = 1.6 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 3.1 μM), Shigella dysentariae ATCC 9752 (MIC = 12.5 μM), Salmonella typhimurium ATCC 14028 (MIC = 6.3 μM), Klebsiella pneumonia ATCC 10031 (MIC = 12.5 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 6.3 μM).	[Ref.26235946] It has 13.5% hemolysis against human red blood cells at 12.5 μM and 25.5% hemolysis at 25 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 ,6, 9 and 13) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (2) and Ⓧ (6), Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	26235946	Bioorg Med Chem Lett. 2015 Sep 15;25(18):4016-9. doi: 10.1016/j.bmcl.2015.06.053. Epub 2015 Jun 19.	Thuy T T Dinh, Do-Hee Kim, Huy X Luong, Bong-Jin Lee, Young-Woo Kim	Antimicrobial activity of doubly-stapled alanine/lysine-based peptides	Stapled AMP						
DRAMP21605	KⓍWKAⓍK	KXWKAXK	KXWKAXK	7	S1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 25 μM), Staphylococcus aureus ATCC 6538p (MIC = 25 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 50 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 50 μM).	It has 0.53%, 0.53%, 0.67%, 0.66%, 0.83%, 1.36%, 1.17% and 1.21% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC	Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim	De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides	Stapled AMP						
DRAMP21607	KⓍAKWⓍK	KXAKWXK	KXAKWXK	7	S2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 50 μM), Staphylococcus aureus ATCC 6538p (MIC = 100 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 50 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM).	It has 0.91%, 1.01%, 0.66%, 0.99%, 0.63%, 0.82%, 1.75% and 1.24% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC	Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim	De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides	Stapled AMP						
DRAMP21609	KⓍWKLⓍK	KXWKLXK	KXWKLXK	7	S3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphylococcus aureus ATCC 6538p (MIC = 25 μM), Staphylococcus epidermis ATCC 12228 (MIC = 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysentariae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumonia ATCC 10031 (MIC = 25 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM).	It has 0.87%, 0.65%, 1.02%, 0.94%, 2.13%, 2.52%, 3.81% and 7.75% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC	Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim	De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides	Stapled AMP						
DRAMP21611	KⓍLKWⓍK	KXLKWXK	KXLKWXK	7	S4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphylococcus aureus ATCC 6538p (MIC = 12.5 μM), Staphylococcus epidermis ATCC 12228 (MIC = 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 25 μM), Shigella dysentariae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumonia ATCC 10031 (MIC = 25 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM).	It has 0.71%, 0.90%, 0.71%, 0.68%, 1.08%, 1.87%, 2.46% and 4.50% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC	Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim	De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides	Stapled AMP						
DRAMP21613	KⓍWAKⓍA	KXWAKXA	KXWAKXA	7	S5	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 50 μM), Staphylococcus aureus ATCC 6538p (MIC = 50 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 50 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM).	It has 0.65%, 0.60%, 0.59%, 0.76%, 0.83%, 0.76%, 0.88% and 1.04% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC	Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim	De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C=O)C)(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21615	KⓍAWKⓍA	KXAWKXA	KXAWKXA	7	S6	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)	As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts.	Not found	Function: Antibacterial activity against Gram-negative bacteria. Antibacterial activity against Gram-positive bacteria is not noteable under 100 μM.	Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC > 100 μM), Staphylococcus aureus ATCC 6538p (MIC > 100 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);##Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 100 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC > 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM).	It has 0.65%, 0.66%, 0.75%, 0.87%, 0.64%, 0.70%, 0.61% and 0.84% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found.	PubMed ID is not available	B KOREAN CHEM SOC	Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim	De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides	Stapled AMP						O=C(NC1(C)C(=O)NC(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C=O)C)(C)CCCC=CCCC1)C([NH3+])CCCC[NH3+]
DRAMP21617	qqrkrkiwsⓚlapⓓgttlvklvagig	qqrkrkiwsklapdgttlvklvagig	qqrkrkiwsilaplgttlvklvagig	26	sDRIM	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①Disordered (or unstructured) conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②50% average α-helix content in various membranes environments [57% in POPC; 67% in POPC/P	In the cases of sDRIM and sKFGF, stapling did not induce any conformational change, as these analogues remained just as unstructured.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC = 128 μg/mL), Enterococcus faecalis (MIC = 64 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 32 μg/mL), Pseudomonas aeruginosa (MIC = 64 μg/mL)	[Ref.28921993] It has 13.4%, 18.6%, 25.4%, 33.4%, 42.0%, 46.9%, 42.2% and 47.1% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml.	Cyclic (Stapled)	Free	Amidation	ⓚ (10) and ⓓ (14) are corss-linked by lactam stapling through the polar amide bond of a lactam bridge.	D	[Ref.28921993] The toxicity of sDRIM toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM.	28921993	J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26.	Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich	Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties.	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NCC=O)C(CC)C)C)C(C)C)CC(C)C)CCCC[NH3+])C(C)C)CC(C)C)C(O)C)C(NC(=O)CNC(=O)C(NC(=O)C1N(C(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])CCC(=O)N)CCC(=O)N)CCCNC(=[NH2+])N)CCCC[NH3+])CCCNC(=[NH2+])N)CCCC[NH3+])C(CC)C)Cc2c3c([nH]c2)cccc3)CO)CCCC[NH3+])CC(C)C)C)CCC1)CC=O)C(O)C
DRAMP21619	PLIⓀLRLⒹRGQF	PLIKLRLDRGQF	PLILLRLLRGQF	12	sWWSP	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①α-helix in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②43% average α-helix content in various membranes environments [38% in POPC; 58% in POPC/POPG(3:1); 47% in POPC:lysoPC(9:1);	On the other hand, sWWSP and sMAP-1 assumed an α-helical conformation in aqueous solution, in contrast to their unstructured linear countparts.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC > 256 μg/mL), Enterococcus faecalis (MIC > 256 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC > 256 μg/mL), Pseudomonas aeruginosa (MIC > 256 μg/mL)	[Ref.28921993] It has 4.0%, 4.8%, 4.6%, 4.2% and 7.0% hemolysis against human red blood cells at 15, 20, 25, 30 and 40 μg/ml.	Cyclic (Stapled)	Free	Amidation	Ⓚ (4) and Ⓓ (8) are cross-linked by lactam stapling through the polar amide bond of a lactam bridge.	L	[Ref.28921993] The toxicity of sWWSP toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM.	28921993	J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26.	Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich	Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties.	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C=O)Cc1ccccc1)CCC(=O)N)CCCNC(=[NH2+])N)CC=O)CC(C)C)CCCNC(=[NH2+])N)CC(C)C)CCCC[NH3+])C(NC(=O)C(NC(=O)C1[NH2+]CCC1)CC(C)C)C(CC)C
DRAMP21621	AAⓀLLPⒹLLAAP	AAKLLPDLLAAP	AAVLLPVLLAAP	12	sKFGF	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①Disordered (or unstructured) conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②Around 22% average α-helix content in various membranes environments [13% in POPC; 32% in	In the cases of sDRIM and sKFGF, stapling did not induce any conformational change, as these analogues remained just as unstructured.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC > 256 μg/mL), Enterococcus faecalis (MIC > 256 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC > 256 μg/mL), Pseudomonas aeruginosa (MIC > 256 μg/mL)	[Ref.28921993] It has 0.4%, 0%, 0.1%, 0.2%, 0.1%, 0.7%, 1.8% and 5.6% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml.	Cyclic (Stapled)	Free	Amidation	Ⓚ (3) and Ⓓ (7) are cross-linked by lactam stapling through the polar amide bond of a lactam bridge.	L	[Ref.28921993] The toxicity of sKFGF toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM.	28921993	J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26.	Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich	Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties.	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)N1C(C=O)CCC1)C)C)CC(C)C)CC(C)C)C(NC(=O)C1N(C(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C)C)CCCC[NH3+])CC(C)C)CC(C)C)CCC1)CC=O
DRAMP21623	KLALKALKⓀLKAⒹLKLA	KLALKALKKLKADLKLA	KLALKALKALKAALKLA	17	sMAP-1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		①α-helix in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②46% average α-helix content in various membranes environments [37% in POPC; 59% in POPC/POPG(3:1); 45% in POPC:lysoPC(9:1);	On the other hand, sWWSP and sMAP-1 assumed an α-helical conformation in aqueous solution, in contrast to their unstructured linear countparts.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC = 64 μg/mL), Enterococcus faecalis (MIC > 256 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 256 μg/mL), Pseudomonas aeruginosa (MIC > 256 μg/mL)	[Ref.28921993] It has 2.5%, 2.9%, 2.4%, 4.1%, 2.9%, 6.3%, 4.9% and 8.2% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml.	Cyclic (Stapled)	Free	Amidation	Ⓚ (9) and Ⓓ (13) are cross-linked by lactam stapling through the polar amide bond of a lactam bridge.	L	[Ref.28921993] The toxicity of sMAP-1 toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM.	28921993	J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26.	Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich	Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties.	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)C)CC(C)C)CCCC[NH3+])CC(C)C)CC=O)C)CCCC[NH3+])CC(C)C)CCCC[NH3+])CCCC[NH3+])CC(C)C)C)CCCC[NH3+])CC(C)C)C)CC(C)C)C([NH3+])CCCC[NH3+]
DRAMP21624	ⓍLAAⒿRHⓍ	XLAAJRHX	ELAAIRHR	8	V30-SP-8	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		26.1% α-helix content in 50 μM aqueous solution [a mixture of water and acetonitrile (9:1, v/v)].	①The helical propensities of two stapled peptides, V30-SP-8 and V30-SP-9, and their linear counterparts were analyzed via circular dichroism (CD) spectrometry. ②Surprisingly, in contrast to our expectation that the stitched peptide, V30-SP-8, would be more helical than the monostapled peptide, V30-SP-9, the monostapling strategy was more effective in inducing helicity (helicity: 26.1% for V30-SP-8 and 33.8% for V30-SP-9)	Not found	Function: Antibacterial activity against Gram-positive bacteria. The peptide shows a similar potency to vancomycin (MIC50 = 20 μM against M.smegmatis)	[Ref.32840352] Gram-positive bacteria: Mycobacterium smegmatis (The antibacterial effects of V30-SP-8 are 36.9%, 42.7%, 50.9% and 55.4% at 6.25, 12.5, 25 and 50 μM, and MIC50 is between 12.5 μM and 25.0 μM)	[Ref.32840352] No hemolytic activity information found.	Cyclic (Stapled)	Free	Free	①The Ⓧ (position: 1 and 8) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓙ (position: 5) in sequence is B5 stapling amino acid. Note: B5 is α-dipentenyl alanine. ③Ⓧ (1) and Ⓙ (5), Ⓙ (5) and Ⓧ (8) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple respectively.	L	No cytotoxicity information found in the reference	32840352	ACS Chem Biol. 2020 Sep 18;15(9):2493-2498. doi: 10.1021/acschembio.0c00492. Epub 2020 Sep 9.	Sung-Min Kang, Heejo Moon, Sang-Woo Han, Do-Hee Kim, Byeong Moon Kim, Bong-Jin Lee	Structure-Based De Novo Design of Mycobacterium Tuberculosis VapC-Activating Stapled Peptides	Stapled AMP						O=C([O-])C1(C)NC(=O)C(Cc2nc[nH]c2)NC(=O)C(CCCNC(=[NH2+])N)NC(=O)C2(NC(=O)C(C)NC(=O)C(C)NC(=O)C(CC(C)C)NC(=O)C([NH3+])(C)CCCC=CCCC2)CCCC=CCCC1
DRAMP21625	ⓏLAAIRHⓍ	ZLAAIRHX	ELAAIRHR	8	V30-SP-9	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		33.8% α-helix content in 50 μM aqueous solution [a mixture of water and acetonitrile (9:1, v/v)].	①The helical propensities of two stapled peptides, V30-SP-8 and V30-SP-9, and their linear counterparts were analyzed via circular dichroism (CD) spectrometry. ②Surprisingly, in contrast to our expectation that the stitched peptide, V30-SP-8, would be more helical than the monostapled peptide, V30-SP-9, the monostapling strategy was more effective in inducing helicity (helicity: 26.1% for V30-SP-8 and 33.8% for V30-SP-9)	Not found	Function: Antibacterial activity against Gram-positive bacteria. 	[Ref.32840352] Gram-positive bacteria: Mycobacterium smegmatis (The antibacterial effects of V30-SP-8 are 23.3%, 23.3%, 34.2% and 38.7% at 6.25, 12.5, 25 and 50 μM, and MIC50 is above 25 μM)	[Ref.32840352] No hemolytic activity information found.	Cyclic (Stapled)	Free	Free	①The Ⓩ (position: 1) in sequence is R8 stapling amino acid. Note: R8 is (R)-octenyl alanine. ②The Ⓧ (position: 8) in sequence is (S)-pentenyl alanine. ③Ⓩ (1) and Ⓧ (8) are cross-linked by hydrocarbon stapling through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	32840352	ACS Chem Biol. 2020 Sep 18;15(9):2493-2498. doi: 10.1021/acschembio.0c00492. Epub 2020 Sep 9.	Sung-Min Kang, Heejo Moon, Sang-Woo Han, Do-Hee Kim, Byeong Moon Kim, Bong-Jin Lee	Structure-Based De Novo Design of Mycobacterium Tuberculosis VapC-Activating Stapled Peptides	Stapled AMP						O=C([O-])C1(C)NC(=O)C(Cc2nc[nH]c2)NC(=O)C(CCCNC(=[NH2+])N)NC(=O)C(C(CC)C)NC(=O)C(C)NC(=O)C(C)NC(=O)C(CC(C)C)NC(=O)C([NH3+])(C)CCCCCCC=CCCC1
DRAMP21628	TLKQFⓍKGVⓍKWLVK	TLKQFXKGVXKWLVK	TLKQFAKGVGKWLVK	15	E2EM15W-S1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		47% α-helical content in a 25 mM potassium phosphate buffer solution at 20 ℃.	①On the other hand, all three stapled analogs of E2EM15W showed substantial increases in helical contents, which again demonstrated the highly effective helix-stabilization through the all-hydrocarbon stapling technology. ②E2EM15W-S1, the most potent analog in the antimicrobial assay, showed the highest degree of helicity (47%) in the aqueous solution, supporting a close correlation between the helicity and the antimicrobial activity of the peptides in this series.	Not found	Function: Antibcaterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria is not noteable under 200 μg/mL.	[Ref.24211019] Gram-positive bacteria: Bacillus subtilis (MIC = 3.13 μg/mL), Staphylococcus aureus (MIC = 3.13 μg/mL), Staphylococcus epidermis (MIC > 200 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC > 200 μg/mL), Shigella dysentariae (MIC > 200 μg/mL), Salmonella typhimurium (MIC > 200 μg/mL), Klebsiella pneumonia (MIC > 200 μg/mL), Proteus mirabilis (MIC > 200 μg/mL), Pseudomonas aeuginose (MIC > 200 μg/mL).	[Ref.24211019] No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl staple.	L	No cytotoxicity information found in the reference	24211019	Bioorg Med Chem Lett. 2013 Dec 15;23(24):6717-20. doi: 10.1016/j.bmcl.2013.10.031. Epub 2013 Oct 26.	Thanh Kim Pham, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Truncated and constrained helical analogs of antimicrobial esculentin-2EM	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NCC(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C(C)C)CC(C)C)Cc2c3c([nH]c2)cccc3)CCCC[NH3+])(C)CCCC=CCCC1)Cc1ccccc1)CCC(=O)N)CCCC[NH3+])CC(C)C)C([NH3+])C(O)C
DRAMP21629	TLKQFⓍKGWⓍKDLVK	TLKQFXKGWXKDLVK	TLKQFAKGVGKWLVK	15	E2EM15W-S2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		27% α-helical content in a 25 mM potassium phosphate buffer solution at 20 ℃.	①On the other hand, all three stapled analogs of E2EM15W showed substantial increases in helical contents, which again demonstrated the highly effective helix-stabilization through the all-hydrocarbon stapling technology. ②Although they bear the oce-4-enyl staple at the same positions as in E2EM15W-S1, the other stapled derivatives E2EM15W-S2 and E2EM15W-S3 exhibited markedly smaller helical contents: 27% and 37%, repectively.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.24211019] Gram-positive bacteria: Bacillus subtilis (MIC = 6.25 μg/mL), Staphylococcus aureus (MIC = 6.25 μg/mL), Staphylococcus epidermis (MIC > 200 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 100 μg/mL), Shigella dysentariae (MIC = 50 μg/mL), Salmonella typhimurium (MIC > 200 μg/mL), Klebsiella pneumonia (MIC = 50 μg/mL), Proteus mirabilis (MIC > 200 μg/mL), Pseudomonas aeuginose (MIC = 200 μg/mL).	[Ref.24211019] No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl staple.	L	No cytotoxicity information found in the reference	24211019	Bioorg Med Chem Lett. 2013 Dec 15;23(24):6717-20. doi: 10.1016/j.bmcl.2013.10.031. Epub 2013 Oct 26.	Thanh Kim Pham, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Truncated and constrained helical analogs of antimicrobial esculentin-2EM	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NCC(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C(C)C)CC(C)C)CC(=O)[O-])CCCC[NH3+])(C)CCCC=CCCC1)Cc1ccccc1)CCC(=O)N)CCCC[NH3+])CC(C)C)C([NH3+])C(O)C
DRAMP21630	TLKQWⓍKGVⓍKDLVK	TLKQWXKGVXKDLVK	TLKQFAKGVGKWLVK	15	E2EM15W-S3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		37% α-helical content in a 25 mM potassium phosphate buffer solution at 20 ℃.	①On the other hand, all three stapled analogs of E2EM15W showed substantial increases in helical contents, which again demonstrated the highly effective helix-stabilization through the all-hydrocarbon stapling technology. ②Although they bear the oce-4-enyl staple at the same positions as in E2EM15W-S1, the other stapled derivatives E2EM15W-S2 and E2EM15W-S3 exhibited markedly smaller helical contents: 27% and 37%, repectively.	Not found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.24211019] Gram-positive bacteria: Bacillus subtilis (MIC = 6.25 μg/mL), Staphylococcus aureus (MIC = 6.25 μg/mL), Staphylococcus epidermis (MIC = 100 μg/mL);##Gram-negative bacteria: Escherichia coli (MIC = 100 μg/mL), Shigella dysentariae (MIC = 50 μg/mL), Salmonella typhimurium (MIC > 200 μg/mL), Klebsiella pneumonia (MIC = 50 μg/mL), Proteus mirabilis (MIC > 200 μg/mL), Pseudomonas aeuginose (MIC > 200 μg/mL).	[Ref.24211019] No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl staple.	L	No cytotoxicity information found in the reference	24211019	Bioorg Med Chem Lett. 2013 Dec 15;23(24):6717-20. doi: 10.1016/j.bmcl.2013.10.031. Epub 2013 Oct 26.	Thanh Kim Pham, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim	Truncated and constrained helical analogs of antimicrobial esculentin-2EM	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NCC(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])C(C)C)CC(C)C)CC(=O)[O-])CCCC[NH3+])(C)CCCC=CCCC1)Cc1c2c([nH]c1)cccc2)CCC(=O)N)CCCC[NH3+])CC(C)C)C([NH3+])C(O)C
DRAMP28986	ⓍIKKⓍLKSAKKFVKAFK	XIKKXLKSAKKFVKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 2 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 3.125 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 1.56 μM), Pseudomonas aeruginosa (MIC = 1.56 μM), 
multiple-drug resistant P.aeruginosa (MIC = 1.56 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 50 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 1 and 5) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (1) and Ⓧ (5) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc1ccccc1)C)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C([NH3+])(C)CCCC=CCCC1)CC(C)C)CCCC[NH3+])CO)C)CCCC[NH3+])CCCC[NH3+])Cc1ccccc1)C(C)C
DRAMP28987	GIKKⓍLKSⓍKKFVKAFK	GIKKXLKSXKKFVKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 3 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 3.125 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 1.56 μM), Pseudomonas aeruginosa (MIC = 3.125 μM), 
multiple-drug resistant P.aeruginosa (MIC = 0.78 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 6.25 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 5 and 9) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (5) and Ⓧ (9) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CO)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc2ccccc2)C)CCCC[NH3+])C(C)C)Cc2ccccc2)CCCC[NH3+])CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP28988	GIKKFLKⓍAKKⓍVKAFK	GIKKFLKXAKKXVKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 4 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 6.25 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 1.56 μM), Pseudomonas aeruginosa (MIC = 1.56 μM), 
multiple-drug resistant P.aeruginosa (MIC = 0.78 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 3.125 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 8 and 12) in sequence indicates (S)-4-pentenyl alanine. ②Ⓧ (8) and Ⓧ (12) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc2ccccc2)C)CCCC[NH3+])C(C)C)(C)CCCC=CCCC1)CCCC[NH3+])CC(C)C)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP28989	GIKKFLKSⓍKKFⓍKAFK	GIKKFLKSXKKFXKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 5 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 12.5 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 1.56 μM), Pseudomonas aeruginosa (MIC = 6.25 μM), 
multiple-drug resistant P.aeruginosa (MIC = 3.125 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 1.56 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 9 and 13) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2ccccc2)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc2ccccc2)C)CCCC[NH3+])(C)CCCC=CCCC1)CO)CCCC[NH3+])CC(C)C)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP28990	GIKKFLKSAKKⓍVKAⓍK	GIKKFLKSAKKXVKAXK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 6 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 3.125 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 1.56 μM), Pseudomonas aeruginosa (MIC = 1.56 μM), 
multiple-drug resistant P.aeruginosa (MIC = 0.78 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 3.125 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 12 and 16) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (12) and Ⓧ (16) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])C)CO)CCCC[NH3+])CC(C)C)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP28991	GIKKⓏLKSAKKⓍVKAFK	GIKKZLKSAKKXVKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 7 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 25 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 3.125 μM), Pseudomonas aeruginosa (MIC = 3.125 μM), 
multiple-drug resistant P.aeruginosa (MIC = 1.56 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 6.25 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓩ (position: 5) in sequence indicates (R)-7-octenyl alanine. ②The Ⓧ (position: 12) in sequence indicates (S)-4-pentenyl alanine. ③ Ⓩ (5) and Ⓧ (12) are cross-linked by hydrocarbon stapling through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CO)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc2ccccc2)C)CCCC[NH3+])C(C)C)(C)CCCC=CCCCCCC1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP28992	GIKKFLKⓏAKKFVKⓍFK	GIKKFLKZAKKFVKXFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 8 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC > 50 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 6.25 μM), Pseudomonas aeruginosa (MIC > 50 μM), 
multiple-drug resistant P.aeruginosa (MIC = 3.125 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 0.19 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓩ (position: 8) in sequence indicates (R)-7-octenyl alanine. ②The Ⓧ (position: 15) in sequence indicates (S)-4-pentenyl alanine. ③ Ⓩ (8) and Ⓧ (15) are cross-linked by hydrocarbon stapling through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2ccccc2)C(=O)NC(C(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])Cc2ccccc2)(C)CCCC=CCCCCCC1)CCCC[NH3+])CC(C)C)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP28993	GIKKFLKSⓏKKFVKAⓍK	GIKKFLKSZKKFVKAXK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide 9 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] All peptides with side-chain stapling showed negative maxima at around 208 and 222 nm, indicating that the peptides formed a stablized helical structure.	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 6.25 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 3.125 μM), Pseudomonas aeruginosa (MIC = 6.25 μM), 
multiple-drug resistant P.aeruginosa (MIC = 3.125 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 3.125 μM	Cyclic (Stapled)	Free	Amidation	①The Ⓩ (position: 9) in sequence indicates (R)-7-octenyl alanine. ②The Ⓧ (position: 16) in sequence indicates (S)-4-pentenyl alanine. ③ Ⓩ (9) and Ⓧ (16) are cross-linked by hydrocarbon stapling through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2ccccc2)C(=O)NC(C(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCCCCC1)CO)CCCC[NH3+])CC(C)C)Cc1ccccc1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C[NH3+])C(CC)C
DRAMP28994	ⓍIKKⓍLKSAKKFVKAFK	XIKKXLKSAKKFVKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide C6-2 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] Peptide C6-2 and C12-2 showed a curve similar to that of peptide 2	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 1.56 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 1.56 μM), Pseudomonas aeruginosa (MIC = 3.125 μM), 
multiple-drug resistant P.aeruginosa (MIC = 3.125 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 12.5 μM	Cyclic (Stapled)	Hexanoylation	Amidation	①The Ⓧ (position: 1 and 5) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (1) and Ⓧ (5) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						
DRAMP28995	ⓍIKKⓍLKSAKKFVKAFK	XIKKXLKSAKKFVKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide C12-2 (Derived from Mag2)	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-helix in 20 mM PBS solution (pH = 7.4) with 1% SDS at peptide concentrations of 100 μM	[Ref.33466998] Peptide C6-2 and C12-2 showed a curve similar to that of peptide 2	Nor found	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC = 6.25 μM). 
##Gram-negative bacteria: Escherichia coli (MIC = 6.25 μM), Pseudomonas aeruginosa (MIC = 12.5 μM), 
multiple-drug resistant P.aeruginosa (MIC = 25 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 0.78 μM	Cyclic (Stapled)	Laurylation	Amidation	①The Ⓧ (position: 1 and 5) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (1) and Ⓧ (5) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						
DRAMP28996	ⓍIKKⓍLKSAKKFVKAFK	XIKKXLKSAKKFVKAFK	GIGKFLHSAKKFGKAFVGEIMNS	17	peptide C18-2 (Derived from Mag2)	No entry found		Synthetic construct	Non-Antimicrobial		Unknown	[Ref.33466998] The circular dichroism (CD) spectral analysis of C18-2 could not be performed because of its poor solubility in the aqueous buffer solution.	Nor found	Function: Antibacterial activity against bacteria is not significant under the concentration of 50 μM.	"[Ref.33466998] Gram-positive bacteria: Staphylococcus aureus (MIC > 50 μM). 
##Gram-negative bacteria: Escherichia coli (MIC > 50 μM), Pseudomonas aeruginosa (MIC > 50 μM), 
multiple-drug resistant P.aeruginosa (MIC > 50 μM)"	[Ref.33466998] It has hemolysis against human red blood cells at 0.78 μM	Cyclic (Stapled)	Stearylation	Amidation	①The Ⓧ (position: 1 and 5) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (1) and Ⓧ (5) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33466998	Molecules. 2021 Jan 16;26(2):444. doi: 10.3390/molecules26020444.	Motoharu Hirano, Chihiro Saito, Hidetomo Yokoo, Chihiro Goto, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence	Stapled AMP						
DRAMP28998	RⓍWWRⓍW	RXWWRXW	RWWWRWW	7	Stapled heptapeptide 2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		Helicity = 61.3% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM	CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides).	Not found	"Function: Antibacterial activity against Gram-positive bacteria.
The stapled peptide was much more active against bacteria than the unstapled one."	Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 19 ± 4 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC > 25 ± 6 μg/mL)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	PubMed ID is not available	Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7.	Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing	De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(C(=O)NC(C=O)Cc2c3c([nH]c2)cccc3)(C)CCCC=CCCC1)C([NH3+])CCCNC(=[NH2+])N
DRAMP29000	WⓍKWWⓍK	WXKWWXK	WWKWWWK	7	Stapled heptapeptide 4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		Helicity = 69.8% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM	CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides).	Not found	"Function: Antibacterial activity against Gram-positive bacteria.
The stapled peptide was much more active against bacteria than the unstapled one."	Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 8.3 ± 1.8 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC = 14 ± 3 μg/mL)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	PubMed ID is not available	Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7.	Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing	De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC1)C([NH3+])Cc1c2c([nH]c1)cccc2
DRAMP29002	LⓍLRLⓍR	LXLRLXR	LLLRLLR	7	Stapled heptapeptide 6	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		Helicity = 75.1% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM	CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides).	Not found	"Function: Antibacterial activity against Gram-positive bacteria.
The stapled peptide was much more active against bacteria than the unstapled one."	Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 24 ± 4 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC = 15 ± 3 μg/mL)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	PubMed ID is not available	Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7.	Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing	De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(CC(C)C)C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C([NH3+])CC(C)C
DRAMP29004	WⓍRRWⓍR	WXRRWXR	WWRRWWR	7	Stapled heptapeptide 8	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+		Helicity = 58.9% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM	CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides).	Not found	"Function: Antibacterial activity against Gram-positive bacteria.
The stapled peptide was much more active against bacteria than the unstapled one."	Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 56 ± 12 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC = 72 ± 18 μg/mL)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	PubMed ID is not available	Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7.	Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing	De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(CCCNC(=[NH2+])N)C(=O)NC(Cc2c3c([nH]c2)cccc3)C(=O)NC(C(=O)NC(C=O)CCCNC(=[NH2+])N)(C)CCCC=CCCC1)C([NH3+])Cc1c2c([nH]c1)cccc2
DRAMP29007	GⓍFAVⓍKKVASVIKGL	GXFAVXKKVASVIKGL	GLFAVIKKVASVIKGL	16	A4K14-citropin1.1-Sp1	No entry found		Synthetic construct	Antimicrobial, Anticancer		Helicity = 89.8% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)	[Ref.33363118] ①CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%. ②Among them, A4K14-citropin 1.1-Sp1 and A4K14-citropin 1.1-Sp4 displayed the top 2 degrees of helicity (89.8 and 85.3%, respectively) in the aqueous solution and acquired 1.46- and 1.38-fold improvements compared to A4K14-citropin 1.1, respectively.	Not found	"Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells.
The hydrolysis enzyme (α-chymotrypsin-mediated) degradation half-life of A4K14-citropin1.1-Sp1  is over 10 hours. A4K14-citropin1.1-Sp1 and A4K14-citropin1.1-Sp4 are much more stable than other A4K14-citropin1.1 stapling derivatives in Ref.33363118."	[Ref.33363118] Cancer cell lines: C4-2B (IC50 = 8.94 μM), A549 (IC50 = 12.48 μM), U87 (IC50 = 11.88 μM), MCF-7 (11.26 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	① The Ⓧ (position: 2 and 6) in sequence indicate (S)-2-(4-pentenyl)alanine. ② Ⓧ (2) and Ⓧ (6) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33363118	Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.	Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						O=C(NC(C(=O)NCC(=O)NC(C=O)CC(C)C)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C(C)C)NC(=O)C(C)NC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)C[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])C(C)C)C)CO)C(C)C)C(CC)C
DRAMP29008	GLFAⓍIKKⓍASVIKGL	GLFAXIKKXASVIKGL	GLFAVIKKVASVIKGL	16	A4K14-citropin1.1-Sp2	No entry found		Synthetic construct	Antimicrobial, Anticancer		Helicity = 66.1% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)	[Ref.33363118] CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%.	Not found	Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells.	[Ref.33363118] Cancer cell lines: C4-2B (IC50 = 10.14 μM), A549 (IC50 = 12.55 μM), U87 (IC50 = 14.76 μM), MCF-7 (12.65 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	① The Ⓧ (position: 5 and 9) in sequence indicate (S)-2-(4-pentenyl)alanine. ② Ⓧ (5) and Ⓧ (9) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33363118	Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.	Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						O=C(NC(C(=O)NCC(=O)NC(C=O)CC(C)C)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C[NH3+])CC(C)C)Cc2ccccc2)C)(C)CCCC=CCCC1)C)CO)C(C)C)C(CC)C
DRAMP29009	GLFAVⓍKKVⓍSVIKGL	GLFAVXKKVXSVIKGL	GLFAVIKKVASVIKGL	16	A4K14-citropin1.1-Sp3	No entry found		Synthetic construct	Antimicrobial, Anticancer		Helicity = 49.2% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)	[Ref.33363118] CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%.	Not found	Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells.	[Ref.33363118] Cancer cell lines: C4-2B (IC50 = 17.89 μM), A549 (IC50 = 12.11 μM), U87 (IC50 = 11.93 μM), MCF-7 (11.92 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	① The Ⓧ (position: 6 and 10) in sequence indicate (S)-2-(4-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33363118	Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.	Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						O=C(NC(C(=O)NCC(=O)NC(C=O)CC(C)C)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(C(C)C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C[NH3+])CC(C)C)Cc2ccccc2)C)C(C)C)(C)CCCC=CCCC1)CO)C(C)C)C(CC)C
DRAMP29010	GLFAVIKKⓍASVⓍKGL	GLFAVIKKXASVXKGL	GLFAVIKKVASVIKGL	16	A4K14-citropin1.1-Sp4	No entry found		Synthetic construct	Antimicrobial, Anticancer		Helicity = 85.3% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)	[Ref.33363118] ①CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%.②Among them, A4K14-citropin 1.1-Sp1 and A4K14-citropin 1.1-Sp4 displayed the top 2 degrees of helicity (89.8 and 85.3%, respectively) in the aqueous solution and acquired 1.46- and 1.38-fold improvements compared to A4K14-citropin 1.1, respectively.	Not found	"Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells.
The hydrolysis enzyme (α-chymotrypsin-mediated) degradation half-life of A4K14-citropin1.1-Sp1  is over 10 hours. A4K14-citropin1.1-Sp1 and A4K14-citropin1.1-Sp4 are much more stable than other A4K14-citropin1.1 stapling derivatives in Ref.33363118."	[Ref.33363118] Cancer cell lines: C4-2B (IC50 = 8.90 μM), A549 (IC50 = 10.51 μM), U87 (IC50 = 7.277 μM), MCF-7 (10.49 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	① The Ⓧ (position: 9 and 13) in sequence indicate (S)-2-(4-pentenyl)alanine. ② Ⓧ (9) and Ⓧ (13) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33363118	Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.	Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C)C(=O)NC(CO)C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C=O)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C[NH3+])CC(C)C)Cc1ccccc1)C)C(C)C)C(CC)C
DRAMP29011	GLFAVIKKVAⓍVIKⓍL	GLFAVIKKVAXVIKXL	GLFAVIKKVASVIKGL	16	A4K14-citropin1.1-Sp5	No entry found		Synthetic construct	Antimicrobial, Anticancer		Helicity = 49.4% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)	[Ref.33363118] CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%.	Not found	Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells.	[Ref.33363118] Cancer cell lines: C4-2B (IC50 = 11.90 μM), A549 (IC50 = 9.899 μM), U87 (IC50 = 8.229 μM), MCF-7 (12.42 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	① The Ⓧ (position: 11 and 15) in sequence indicate (S)-2-(4-pentenyl)alanine. ② Ⓧ (11) and Ⓧ (15) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	33363118	Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.	Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NC(C(C)C)C(=O)NC(C(CC)C)C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C=O)CC(C)C)(C)CCCC=CCCC1)C)C(C)C)CCCC[NH3+])CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C[NH3+])CC(C)C)Cc1ccccc1)C)C(C)C)C(CC)C
DRAMP29012	GⓏFAVIKKⓍASVIKGL	GZFAVIKKXASVIKGL	GLFAVIKKVASVIKGL	16	A4K14-citropin1.1-Sp6	No entry found		Synthetic construct	Antimicrobial, Anticancer		Helicity = 34.9% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)	[Ref.33363118] CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%.	Not found	Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells.	[Ref.33363118] Cancer cell lines: C4-2B (IC50 = 35.84 μM), A549 (IC50 = 30.19 μM), U87 (IC50 = 34.49 μM), MCF-7 (23.78 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	① The Ⓩ (position: 2) in sequence indicates (R)-2-(7-octenyl)alanine. ② The Ⓧ (position: 9) in sequence indicates (S)-2-(4-pentenyl)alanine. ③ Ⓩ and Ⓧ are cross-linked by ring-closing metathesis through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	33363118	Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.	Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						O=C(NC(C(=O)NCC(=O)NC(C=O)CC(C)C)CCCC[NH3+])C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(C(C)C)NC(=O)C(C)NC(=O)C(Cc2ccccc2)NC(=O)C(NC(=O)C[NH3+])(C)CCCCCCC=CCCC1)C)CO)C(C)C)C(CC)C
DRAMP29013	GLFAVⓏKKVASVⓍKGL	GLFAVZKKVASVXKGL	GLFAVIKKVASVIKGL	16	A4K14-citropin1.1-Sp7	No entry found		Synthetic construct	Antimicrobial, Anticancer		Helicity = 13.6% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)	[Ref.33363118] CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%.	Not found	Function: Antitumor activity against A549, HCT116 and HepG2 cancer cells.	[Ref.33363118] Cancer cell lines: C4-2B (IC50 = 10.23 μM), A549 (IC50 = 16.37 μM), U87 (IC50 = 14.72 μM), MCF-7 (12.1 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	① The Ⓩ (position: 6) in sequence indicates (R)-2-(7-octenyl)alanine. ② The Ⓧ (position: 13) in sequence indicates (S)-2-(4-pentenyl)alanine. ③ Ⓩ and Ⓧ are cross-linked by ring-closing metathesis through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	33363118	Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.	Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						O=C(NC1(C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(C)C)C(=O)NC(C)C(=O)NC(CO)C(=O)NC(C(C)C)C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C=O)CC(C)C)CCCC[NH3+])(C)CCCC=CCCCCCC1)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C[NH3+])CC(C)C)Cc1ccccc1)C)C(C)C
DRAMP29015	IKLSPⓍTKDⓍLKKVLKGAIKGAIAVAKMV	IKLSPXTKDXLKKVLKGAIKGAIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-2	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 4.26 ± 0.52 μM), HCT116 (IC50 = 3.54 ± 0.72 μM), HepG2 (IC50 = 1.60 ± 0.24 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 6 and 10) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CC(=O)[O-])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C2N(C(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCC2)(C)CCCC=CCCC1)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])C)C(CC)C)CCCC[NH3+])C)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29016	IKLSPETKDNLKKVLKGⓍIKGⓍIAVAKMV	IKLSPETKDNLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-5	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 7.35 ± 0.22 μM), HCT116 (IC50 = 4.16 ± 0.21 μM), HepG2 (IC50 = 2.82 ± 0.23 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 18 and 22) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C2N(C(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCC2)CCC(=O)[O-])C(O)C)CCCC[NH3+])CC(=O)[O-])CC(=O)N)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29017	IKLSPⓍTKDⓍLKKVLKGⓍIKGⓍIAVAKMV	IKLSPXTKDXLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-10	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 3.59 ± 0.12 μM), HCT116 (IC50 = 3.51 ± 0.37 μM), HepG2 (IC50 = 1.50 ± 0.21 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 6, 10, 18 and 22) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10), Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple, respectively.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C2(C)NC(=O)C(CC(=O)[O-])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C3N(C(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCC3)(C)CCCC=CCCC2)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29019	IKLSKⓍTKDⓍLKKVLKGAIKGAIAVAKMV	IKLSKXTKDXLKKVLKGAIKGAIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-15	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 2.26 ± 0.24 μM), HCT116 (IC50 = 2.95 ± 0.25 μM), HepG2 (IC50 = 2.20 ± 0.27 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 6 and 10) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CC(=O)[O-])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCCC[NH3+])(C)CCCC=CCCC1)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])C)C(CC)C)CCCC[NH3+])C)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29020	IKLSPⓍTKKⓍLKKVLKGAIKGAIAVAKMV	IKLSPXTKKXLKKVLKGAIKGAIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-16	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 1.85 ± 0.31 μM), HCT116 (IC50 = 2.65 ± 0.35 μM), HepG2 (IC50 = 3.14 ± 0.46 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 6 and 10) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C2N(C(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCC2)(C)CCCC=CCCC1)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])C)C(CC)C)CCCC[NH3+])C)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29021	IKLSKⓍTKKⓍLKKVLKGAIKGAIAVAKMV	IKLSKXTKKXLKKVLKGAIKGAIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-17	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 0.96 ± 0.33 μM), HCT116 (IC50 = 1.49 ± 0.45 μM), HepG2 (IC50 = 1.64 ± 0.47 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 6 and 10) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCCC[NH3+])(C)CCCC=CCCC1)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])C)C(CC)C)CCCC[NH3+])C)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29022	IKLSKKTKKNLKKVLKGⓍIKGⓍIAVAKMV	IKLSKKTKKNLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-18	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 0.89 ± 0.21 μM), HCT116 (IC50 = 1.11 ± 0.21 μM), HepG2 (IC50 = 1.61 ± 0.21 μM)	[Ref.30789695] It has -1.5%, 3.8%, 12.8%, 18.2%, 13.8%, 30.2%, 65.2%, 90.8% and 83.5% hemolysis against fresh rabbit blood cells at 0.010, 0.25, 0.5, 1.0, 2.0, 5.0, 10.0, 20.0 and 25.0 μM.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 18 and 22) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCCC[NH3+])(C)CCCC=CCCC1)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])C)C(CC)C)CCCC[NH3+])C)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29023	IKLSKETKKNLKKVLKGⓍIKGⓍIAVAKMV	IKLSKETKKNLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-19	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 1.00 ± 0.36 μM), HCT116 (IC50 = 1.78 ± 0.35 μM), HepG2 (IC50 = 1.64 ± 0.36 μM)	[Ref.30789695] It has 1.8%, 11.5%, 22.2%, 20.5%, 16.2%, 39.5%, 69.2%, 94.8% and 102.5% hemolysis against fresh rabbit blood cells at 0.010, 0.25, 0.5, 1.0, 2.0, 5.0, 10.0, 20.0 and 25.0 μM.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 18 and 22) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCCC[NH3+])CCC(=O)[O-])C(O)C)CCCC[NH3+])CCCC[NH3+])CC(=O)N)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29024	IKLSPⓍTKKⓍLKKVLKGⓍIKGⓍIAVAKMV	IKLSPXTKKXLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-20	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 2.10 ± 0.32 μM), HCT116 (IC50 = 2.63 ± 0.35 μM), HepG2 (IC50 = 4.93 ± 0.53 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 6, 10, 18 and 22) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10), Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple, respectively.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C2(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C3N(C(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCC3)(C)CCCC=CCCC2)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29025	IKLSKⓍTKKⓍLKKVLKGⓍIKGⓍIAVAKMV	IKLSKXTKKXLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-21	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 3.26 ± 0.36 μM), HCT116 (IC50 = 3.05 ± 0.21 μM), HepG2 (IC50 = 1.50 ± 0.28 μM)	No hemolytic activity information found.	Cyclic (Stapled)	Free	Amidation	① The Ⓧ (position: 6, 10, 18 and 22) in sequence indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ② Ⓧ (6) and Ⓧ (10), Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple, respectively.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C2(C)NC(=O)C(CCCC[NH3+])NC(=O)C(CCCC[NH3+])NC(=O)C(C(O)C)NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)CO)CCCC[NH3+])(C)CCCC=CCCC2)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29026	IKLSKETKKNLKKVLKGⓍIKGⓍIAVAKMV	IKLSKETKKNLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-57	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 1.10 ± 0.31 μM), HCT116 (IC50 = 1.65 ± 0.28 μM), HepG2 (IC50 = 2.71 ± 0.05 μM)	[Ref.30789695] It has -1.2%, 1.8%, 2.8%, 5.5%, 14.5%, 25.8%, 42.8%, 68.8% and 58.2% hemolysis against fresh rabbit blood cells at 0.010, 0.25, 0.5, 1.0, 2.0, 5.0, 10.0, 20.0 and 25.0 μM.	Cyclic (Stapled)	Free	Amidation	① The S (position: 4), T (position: 7) and N (position: 10) in sequence are linked with N-acetylglucosamine (GlcNAc), respectively. ② The Ⓧ (position: 18 and 22) indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ③ Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple, respectively.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)COC2C(NC(=O)C)C(O)C(O)C(CO)O2)CCCC[NH3+])CCC(=O)[O-])C(OC(OC(CO)CO)C(NC(=O)C)CO)C)CCCC[NH3+])CCCC[NH3+])CC(=O)NC2C(NC(=O)C)C(O)C(O)C(CO)O2)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29027	IKLSKKTKKNLKKVLKGⓍIKGⓍIAVAKMV	IKLSKKTKKNLKKVLKGXIKGXIAVAKMV	IKLSPETKDNLKKVLKGAIKGAIAVAKMV	29	H-58	No entry found		Synthetic construct	Antimicrobial, Anticancer		α-helical (most likely)	No detailed structure description found.	Not found	"Function: Anticancer activity. 
Ref.30789695 does not include results of antimicrobial, hemolysis and other biological assays"	[Ref.30789695] Cancer cell lines: A549 (IC50 = 0.62 ± 0.12 μM), HCT116 (IC50 = 1.29 ± 0.08 μM), HepG2 (IC50 = 2.13 ± 0.07 μM)	[Ref.30789695] It has 0.8%, -0.5%, 0.8%, 8.8%, 13.2%, 20.8%, 37.8%, 61.8% and 54.5% hemolysis against fresh rabbit blood cells at 0.010, 0.25, 0.5, 1.0, 2.0, 5.0, 10.0, 20.0 and 25.0 μM.	Cyclic (Stapled)	Free	Amidation	① The S (position: 4), T (position: 7) and N (position: 10) in sequence are linked with N-acetylglucosamine (GlcNAc), respectively. ② The Ⓧ (position: 18 and 22) indicate (S)-N-Fmoc-2-(4'-pentenyl)alanine. ③ Ⓧ (18) and Ⓧ (22) are cross-linked by ring-closing metathesis through an oct-4-enyl hydrocarbon staple, respectively.	L	No cytotoxicity information found in the reference	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. doi: 10.1021/acschembio.9b00046. Epub 2019 Mar 1.	Yulei Li, Yihan Zhang, Minghao Wu, Qi Chang, Honggang Hu, Xia Zhao	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						S(CCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C1(C)NC(=O)CNC(=O)C(CCCC[NH3+])NC(=O)C(C(CC)C)NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C([NH3+])C(CC)C)CCCC[NH3+])CC(C)C)COC2C(NC(=O)C)C(O)C(O)C(CO)O2)CCCC[NH3+])CCCC[NH3+])C(OC2C(NC(=O)C)C(O)C(O)C(CO)O2)C)CCCC[NH3+])CCCC[NH3+])CC(=O)NC2C(NC(=O)C)C(O)C(O)C(CO)O2)CC(C)C)CCCC[NH3+])CCCC[NH3+])C(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCC1)C(CC)C)C)C(C)C)C)CCCC[NH3+])C(=O)NC(C=O)C(C)C)C
DRAMP29032	KLLKKAGKLLKKⓏGKLLKKⓍG	KLLKKAGKLLKKZGKLLKKXG	KLLKKAGKLLKKAGKLLKKAG	21	Stripe-based foldamer peptide 4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-Helix content = 39% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate	[Ref.33369262] As shown in Figure 2, peptides 2, 3, 4 and 5 showed negative maxima at around 208 and 222nm, which suggests that they formed stable α-helical structures, similar to Stripe.	Not found	"Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.
It is a helical foldmer peptide based on ""Stripe"" (an AMP manually designed) by introducing a hydrocarbon stapling. The peptide showed weaker activity than Stripe."	[Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC = 25 μM) ;##Gram-negative bacteria: Escherichia coli DH5α (MIC = 6.25 μM), Pseudomonas aeruginosa NBRC13275 (MIC = 50 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC = 25 μM)	[Ref.33369262] It exhibits hemolysis at 0.78 μM agasint human red blood cells.	Cyclic (Stapled)	Free	Free	①The Ⓩ (position: 13) in sequence denotes (R)-(7-octenyl)alanine. ②The Ⓧ (position: 20) in sequence denotes (S)-(4-pentenyl)alanine. ③ Ⓩ (13) and Ⓧ (20) are cross-linked by side-stapling through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	33369262	Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749.	Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NCC(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NCC(=O)[O-])(C)CCCC=CCCCCCC1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CC(C)C)CCCC[NH3+])C)CCCC[NH3+])CCCC[NH3+])CC(C)C)CC(C)C)C([NH3+])CCCC[NH3+]
DRAMP29033	KLLKKⓏGKLLKKⓍGKLLKKAG	KLLKKZGKLLKKXGKLLKKAG	KLLKKAGKLLKKAGKLLKKAG	21	Stripe-based foldamer peptide 5	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		α-Helix content = 34% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate	[Ref.33369262] As shown in Figure 2, peptides 2, 3, 4 and 5 showed negative maxima at around 208 and 222nm, which suggests that they formed stable α-helical structures, similar to Stripe.	Not found	"Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.
It is a helical foldmer peptide based on ""Stripe"" (an AMP manually designed) by introducing a hydrocarbon stapling. The peptide showed weaker activity than Stripe."	[Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC = 25 μM) ;##Gram-negative bacteria: Escherichia coli DH5α (MIC = 6.25 μM), Pseudomonas aeruginosa NBRC13275 (MIC = 12.5 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC = 25 μM)	[Ref.33369262] It exhibits hemolysis at 1.56 μM agasint human red blood cells.	Cyclic (Stapled)	Free	Free	①The Ⓩ (position: 6) in sequence denotes (R)-(7-octenyl)alanine. ②The Ⓧ (position: 13) in sequence denotes (S)-(4-pentenyl)alanine. ③ Ⓩ (6) and Ⓧ (13) are cross-linked by side-stapling through a undec-4-enyl staple.	L	No cytotoxicity information found in the reference	33369262	Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749.	Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu	Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling	Stapled AMP						O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC1(C)C(=O)NCC(=O)NC(CCCC[NH3+])C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)[O-])C)CCCC[NH3+])CCCC[NH3+])CC(C)C)CC(C)C)CCCC[NH3+])(C)CCCC=CCCCCCC1)CCCC[NH3+])CCCC[NH3+])CC(C)C)CC(C)C)C([NH3+])CCCC[NH3+]
DRAMP29235	TIEEQAKTⓍLDKⓍNHEAEDLFYQⓍSLAⓍWN	TIEEQAKTXLDKXNHEAEDLFYQXSLAXWN	TIEEQAKTFLDKFNHEAEDLFYQSSLASWN	30	NYBSP-1	No entry found		Synthetic construct	Antimicrobial, Antiviral(SARS-CoV-2)		94% α-helical content in 10 mM phosphate-buffered saline (PBS)	No other descriptive information about the structure found in the literature	Not found	Mechanism of action:The stapled peptide designed based on the ACE2 helix, which is expected to bind to SARS-CoV-2 and prevent the binding of the virus to the ACE2 receptor and disrupt the infection.	[Ref.33310780]Virus:##SARS-CoV-2:Inhibition of infection in HT1080/ACE2 cells(IC50=4.1 ± 0.26 μM);Inhibition of infection in A549/ACE2 cells(IC50=2.2 ± 0.14 μM);Inhibition of virus-induced cytopathic effect (CPE) in Vero E6 cells(IC100=17.2 μM);##VSV-G:Inhibition of infection in HT1080/ACE2 cells(IC50>27.5 μM);Inhibition of infection in A549/ACE2 cells(IC50>27.5 μM).	No hemolytic activity information found.	Cyclic (Stapled)	Acylation	Amidation	①The Ⓧ (position: 9,13,24 and 28) in sequence indicate S-2-(4'-pentenyl) alanine.② Ⓧ(9) and Ⓧ(13), Ⓧ(24) and Ⓧ(28) are cross-linked by hydrocarbon stapling.	L	[Ref.33310780]HT1080/ACE2 cells:CC50>27.5 μM(Less than 10% toxicity at this dose);A549/ACE2 cells:CC50>27.5 μM(Less than 10% toxicity at this dose).	33310780	mBio. 2020 Dec 11;11(6):e02451-20.	Curreli F, Victor SMB, Ahmed S, Drelich A, Tong X, Tseng CK, Hillyer CD, Debnath AK.	Stapled Peptides Based on Human Angiotensin-Converting Enzyme 2 (ACE2) Potently Inhibit SARS-CoV-2 Infection In Vitro.	Stapled AMP						
DRAMP29236	TIEEQⓏKTFLDKⓍNHEAEDLⓏYQSSLAⓍWN	TIEEQZKTFLDKXNHEAEDLZYQSSLAXWN	TIEEQAKTFLDKFNHEAEDLFYQSSLASWN	30	NYBSP-2	No entry found		Synthetic construct	Antimicrobial, Antiviral(SARS-CoV-2)		61% α-helical content in 10 mM phosphate-buffered saline (PBS)	No other descriptive information about the structure found in the literature	Not found	Mechanism of action:The stapled peptide designed based on the ACE2 helix, which is expected to bind to SARS-CoV-2 and prevent the binding of the virus to the ACE2 receptor and disrupt the infection.	[Ref.33310780]Virus:##SARS-CoV-2:Inhibition of infection in HT1080/ACE2 cells(IC50=2.9 ± 0.27 μM);Inhibition of infection in A549/ACE2 cells(IC50=2.68 ± 0.14 μM);Inhibition of virus-induced cytopathic effect (CPE) in Vero E6 cells(IC100=33.5 μM);##VSV-G:Inhibition of infection in HT1080/ACE2 cells(IC50>26.8 μM);Inhibition of infection in A549/ACE2 cells(IC50>26.8 μM).	No hemolytic activity information found.	Cyclic (Stapled)	Acylation	Amidation	①The Ⓧ(position: 13 and 28) in sequence indicate S-2-(4'-pentenyl) alanine.②The Ⓩ(position: 6 and 21) indicate 2-(7'-octenyl) alanine in the R configuration.③ Ⓩ(6) and Ⓧ(13), Ⓩ(21) and Ⓧ(28) are cross-linked by hydrocarbon stapling.	L	[Ref.33310780]HT1080/ACE2 cells:CC50>26.8 μM(Less than 10% toxicity at this dose);A549/ACE2 cells:CC50>26.8 μM(Less than 10% toxicity at this dose).	33310780	mBio. 2020 Dec 11;11(6):e02451-20.	Curreli F, Victor SMB, Ahmed S, Drelich A, Tong X, Tseng CK, Hillyer CD, Debnath AK.	Stapled Peptides Based on Human Angiotensin-Converting Enzyme 2 (ACE2) Potently Inhibit SARS-CoV-2 Infection In Vitro.	Stapled AMP						
DRAMP29237	TIEEQAKTⓍLDKⓍNHEAEDLⓏYQSSLAⓍWN	TIEEQAKTXLDKXNHEAEDLZYQSSLAXWN	TIEEQAKTFLDKFNHEAEDLFYQSSLASWN	30	NYBSP-3	No entry found		Synthetic construct	Antimicrobial, Antiviral(SARS-CoV-2)		50% α-helical content in 10 mM phosphate-buffered saline (PBS)	No other descriptive information about the structure found in the literature	Not found	Mechanism of action:The stapled peptide designed based on the ACE2 helix, which is expected to bind to SARS-CoV-2 and prevent the binding of the virus to the ACE2 receptor and disrupt the infection.	[Ref.33310780]Virus:##SARS-CoV-2:Inhibition of infection in HT1080/ACE2 cells(IC50=12.9 ± 0.35 μM);Inhibition of infection in A549/ACE2 cells(IC50~25 μM);##VSV-G:Inhibition of infection in HT1080/ACE2 cells(IC50>27.6 μM);Inhibition of infection in A549/ACE2 cells(IC50>27.6 μM).	No hemolytic activity information found.	Cyclic (Stapled)	Acylation	Amidation	①The Ⓧ (position: 9,13 and 28) in sequence indicate S-2-(4'-pentenyl) alanine.②The Ⓩ (position: 21) indicates 2-(7'-octenyl) alanine in the R configuration.③ Ⓧ(9) and Ⓧ(13), Ⓩ(21) and Ⓧ(28) are cross-linked by hydrocarbon stapling.	L	[Ref.33310780]HT1080/ACE2 cells:CC50>27.6 μM(Less than 10% toxicity at this dose);A549/ACE2 cells:CC50>27.6 μM(Less than 10% toxicity at this dose).	33310780	mBio. 2020 Dec 11;11(6):e02451-20.	Curreli F, Victor SMB, Ahmed S, Drelich A, Tong X, Tseng CK, Hillyer CD, Debnath AK.	Stapled Peptides Based on Human Angiotensin-Converting Enzyme 2 (ACE2) Potently Inhibit SARS-CoV-2 Infection In Vitro.	Stapled AMP						
DRAMP29238	TIEEQⓏKTFLDKⓍNHEAEDLFYQⓍSLAⓍWN	TIEEQZKTFLDKXNHEAEDLFYQXSLAXWN	TIEEQAKTFLDKFNHEAEDLFYQSSLASWN	30	NYBSP-4	No entry found		Synthetic construct	Antimicrobial, Antiviral(SARS-CoV-2)		80% α-helical content in 10 mM phosphate-buffered saline (PBS)	No other descriptive information about the structure found in the literature	Not found	Mechanism of action:Proteolytic stability of NYBSP-4 in human plasma(half-life (T1/2) of NYBSP-4 was >289 min).The stapled peptide designed based on the ACE2 helix, which is expected to bind to SARS-CoV-2 and prevent the binding of the virus to the ACE2 receptor and disrupt the infection.	[Ref.33310780]Virus:##SARS-CoV-2:Inhibition of infection in HT1080/ACE2 cells(IC50=1.97 ± 0.14 μM);Inhibition of infection in A549/ACE2 cells(IC50=2.8 ± 0.08 μM);Inhibition of virus-induced cytopathic effect (CPE) in Vero E6 cells(IC100=33 μM);##VSV-G:Inhibition of infection in HT1080/ACE2 cells(IC50>26.6 μM);Inhibition of infection in A549/ACE2 cells(IC50>26.6 μM).	No hemolytic activity information found.	Cyclic (Stapled)	Acylation	Amidation	①The Ⓧ (position: 13,24 and 28) in sequence indicate S-2-(4'-pentenyl) alanine.②The Ⓩ (position: 6) indicates 2-(7'-octenyl) alanine in the R configuration.③  Ⓩ(6) and Ⓧ(13), Ⓧ(24) and Ⓧ(28) are cross-linked by hydrocarbon stapling.	L	[Ref.33310780]HT1080/ACE2 cells:CC50>26.6 μM(Less than 10% toxicity at this dose);A549/ACE2 cells:CC50>26.6 μM(Less than 10% toxicity at this dose).	33310780	mBio. 2020 Dec 11;11(6):e02451-20.	Curreli F, Victor SMB, Ahmed S, Drelich A, Tong X, Tseng CK, Hillyer CD, Debnath AK.	Stapled Peptides Based on Human Angiotensin-Converting Enzyme 2 (ACE2) Potently Inhibit SARS-CoV-2 Infection In Vitro.	Stapled AMP						
DRAMP29239	IEEQAKTFLDKFNHEⓀEDLⒺYQSSLASWNYNTNIT	IEEQAKTFLDKFNHEKEDLEYQSSLASWNYNTNIT	IEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNIT	35	hACE2(21-55)A36K-F40E	No entry found		Synthetic construct	Antimicrobial, Antiviral(SARS-CoV-2)		①52% α-helical content in 10 mM PBS at pH 7.4 with 30% TFE at 298 K.②6-13% α-helical content in 10 mM PBS at pH 7.4 and 298 K.	Low helicity for stapled hACE2 peptides in absence of TFE, with predictors of helicity averaging to 6-13% helical content. In the presence of TFE, α-helical structures can be observed for various synthetic hACE2 peptides with predictors averaging from 11 to 52% helical content	Not found	Mechanism of action:The stapled peptide inhibit the RBD-hACE2 complex formation, and hACE2 α1-helix-based peptidomimetics could potentially prevent SARS-CoV-2 from entering the human cells through hACE2 and thus inhibit subsequent viral replication. 	[Ref.33651072]Virus:SARS-CoV-2:inhibition of SARS-CoV-2 Spike protein-hACE2 complex formation(IC50=3.6 μM).	No hemolytic activity information found.	Cyclic (Stapled)	Free	Free	Ⓚ (16) and Ⓔ (20) are corss-linked by lactam stapling.	L	No cytotoxicity information found in the reference(s) presented	33651072	Chem Commun (Camb). 2021 Apr 4;57(26):3283-3286.	Maas MN , Hintzen JCJ , Löffler PMG , Mecinović J . 	Targeting SARS-CoV-2 spike protein by stapled hACE2 peptides.	Stapled AMP						
DRAMP29240	IEEQAKTFLDKⓀNHEⒺEDLFYQSSLASWNYNTNIT	IEEQAKTFLDKKNHEEEDLFYQSSLASWNYNTNIT	IEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNIT	35	hACE2(21-55)F32K-A36E	No entry found		Synthetic construct	Antimicrobial, Antiviral(SARS-CoV-2)		①6-13% α-helical content in 10 mM PBS at pH 7.4 and 298 K.②11-52% α-helical content in 10 mM PBS at pH 7.4 with 30% TFE at 298 K.	Low helicity for stapled hACE2 peptides in absence of TFE, with predictors of helicity averaging to 6-13% helical content. In the presence of TFE, α-helical structures can be observed for various synthetic hACE2 peptides with predictors averaging from 11 to 52% helical content	Not found	Mechanism of action:The stapled peptide inhibit the RBD-hACE2 complex formation, and hACE2 α1-helix-based peptidomimetics could potentially prevent SARS-CoV-2 from entering the human cells through hACE2 and thus inhibit subsequent viral replication. 	[Ref.33651072]Virus:SARS-CoV-2:inhibition of SARS-CoV-2 Spike protein-hACE2 complex formation(IC50=28.4 μM).	No hemolytic activity information found.	Cyclic (Stapled)	Free	Free	Ⓚ (12) and Ⓔ (16) are corss-linked by lactam stapling.	L	No cytotoxicity information found in the reference(s) presented	33651072	Chem Commun (Camb). 2021 Apr 4;57(26):3283-3286.	Maas MN , Hintzen JCJ , Löffler PMG , Mecinović J . 	Targeting SARS-CoV-2 spike protein by stapled hACE2 peptides.	Stapled AMP						
DRAMP29241	IEEQAKTⓀLDKⒺNHEAEDLFYQSSLASWNYNTNIT	IEEQAKTKLDKENHEAEDLFYQSSLASWNYNTNIT	IEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNIT	35	hACE2(21-55)F28K-F32E	No entry found		Synthetic construct	Antimicrobial, Antiviral(SARS-CoV-2)		①6-13% α-helical content in 10 mM PBS at pH 7.4 and 298 K.②11-52% α-helical content in 10 mM PBS at pH 7.4 with 30% TFE at 298 K.	Low helicity for stapled hACE2 peptides in absence of TFE, with predictors of helicity averaging to 6-13% helical content. In the presence of TFE, α-helical structures can be observed for various synthetic hACE2 peptides with predictors averaging from 11 to 52% helical content	Not found	Mechanism of action:The stapled peptide inhibit the RBD-hACE2 complex formation, and hACE2 α1-helix-based peptidomimetics could potentially prevent SARS-CoV-2 from entering the human cells through hACE2 and thus inhibit subsequent viral replication. 	[Ref.33651072]Virus:SARS-CoV-2:inhibition of SARS-CoV-2 Spike protein-hACE2 complex formation(IC50=46.8 μM).	No hemolytic activity information found.	Cyclic (Stapled)	Free	Free	Ⓚ (8) and Ⓔ (12) are corss-linked by lactam stapling.	L	No cytotoxicity information found in the reference(s) presented	33651072	Chem Commun (Camb). 2021 Apr 4;57(26):3283-3286.	Maas MN , Hintzen JCJ , Löffler PMG , Mecinović J . 	Targeting SARS-CoV-2 spike protein by stapled hACE2 peptides.	Stapled AMP						
DRAMP29334	FFGSVLⓀLIPⓀIL	FFGSVLKLIPKIL	FFGSVLKLIPKIL	13	LS-Temporin-Pta	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=4 μg/mL), Staphylococcus aureus BNCC 186335(MIC=4 μg/mL), Staphylococcus aureus(MRSA)(MIC=4 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC>128 μg/mL), E. coli(MIC=64 μg/mL), Cephalosporin-resistant E. coli(MIC=128 μg/mL).	[Ref.34968054]MHC=32 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 7 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (7) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	"[Ref.34968054]Human embryonic kidney HEK293T cells: LC90=64	µg/ml."	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29335	GFKDLLKGAAⓀALVⓀTVLF	GFKDLLKGAAKALVKTVLF	GFKDLLKGAAKALVKTVLF	19	LS-Ascaphin-8 P1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=4 μg/mL), Staphylococcus aureus BNCC 186335(MIC=2 μg/mL),  Staphylococcus aureus(MRSA)(MIC=8 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=128 μg/mL), E. coli(MIC=8 μg/mL), Cephalosporin-resistant E. coli(MIC=16 μg/mL).	[Ref.34968054]MHC=32 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 11 and 15) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (11) and Ⓚ (15) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC90=128 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29336	GFKDLLⓀGAAⓀALVKTVLF	GFKDLLKGAAKALVKTVLF	GFKDLLKGAAKALVKTVLF	19	LS-Ascaphin-8 P2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=8μg/mL), Staphylococcus aureus BNCC 186335(MIC=2 μg/mL),  Staphylococcus aureus(MRSA)(MIC=8 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=32 μg/mL), E. coli(MIC=16 μg/mL), Cephalosporin-resistant E. coli(MIC=32 μg/mL).	[Ref.34968054]MHC=32 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 7 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (7) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC90=128 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29337	GFⓀDLLⓀGAAKALVKTVLF	GFKDLLKGAAKALVKTVLF	GFKDLLKGAAKALVKTVLF	19	LS-Ascaphin-8 P3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=16 μg/mL), Staphylococcus aureus BNCC 186335(MIC=4 μg/mL),  Staphylococcus aureus(MRSA)(MIC=16 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=128 μg/mL), E. coli(MIC=16 μg/mL), Cephalosporin-resistant E. coli(MIC=32 μg/mL).	[Ref.34968054]MHC=32 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 3 and 7) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (3) and Ⓚ (7) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC50=100 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29338	FFGKVLⓀLIRⓀIF	FFGKVLKLIRKIF	FFGKVLKLIRKIF	13	LS-DASamP1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=8μg/mL), Staphylococcus aureus BNCC 186335(MIC=16 μg/mL),  Staphylococcus aureus(MRSA)(MIC=32 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC>128 μg/mL), E. coli(MIC=128 μg/mL), Cephalosporin-resistant E. coli(MIC=128 μg/mL).	[Ref.34968054]MHC=16 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 7 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (7) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC50=128 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29339	PKILNⓀILGⓀILRLAAAFK	PKILNKILGKILRLAAAFK	PKILNKILGKILRLAAAFK	19	LS-PaDBS1R1-1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=2 μg/mL), Staphylococcus aureus BNCC 186335(MIC=2 μg/mL),  Staphylococcus aureus(MRSA)(MIC=4 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=16 μg/mL), E. coli(MIC=4 μg/mL), Cephalosporin-resistant E. coli(MIC=8 μg/mL).	[Ref.34968054]MHC=16 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 6 and 10) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (6) and Ⓚ (10) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC90=128 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29340	PⓀILNⓀILGKILRLAAAFK	PKILNKILGKILRLAAAFK	PKILNKILGKILRLAAAFK	19	LS-PaDBS1R1-2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=4 μg/mL), Staphylococcus aureus BNCC 186335(MIC=4 μg/mL),  Staphylococcus aureus(MRSA)(MIC=4 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=128 μg/mL), E. coli(MIC=16 μg/mL), Cephalosporin-resistant E. coli(MIC=16 μg/mL).	[Ref.34968054]MHC=16 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 2 and 6) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (2) and Ⓚ (6) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC50=100 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29341	VKRFKⓀFFRⓀFKKFV	VKRFKKFFRKFKKFV	VKRFKKFFRKFKKFV	15	LS-Cathelicidin-BF-15-a1-1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=4μg/mL), Staphylococcus aureus BNCC 186335(MIC=2 μg/mL),  Staphylococcus aureus(MRSA)(MIC=2 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=16 μg/mL), E. coli(MIC=2 μg/mL), Cephalosporin-resistant E. coli(MIC=8 μg/mL).	[Ref.34968054]MHC>128 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 6 and 10) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (6) and Ⓚ (10) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	"[Ref.34968054]Human embryonic kidney HEK293T cells: LC50=64	µg/ml."	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29342	VⓀRFKⓀFFRKFKKFV	VKRFKKFFRKFKKFV	VKRFKKFFRKFKKFV	15	LS-Cathelicidin-BF-15-a1-2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=16μg/mL), Staphylococcus aureus BNCC 186335(MIC=2 μg/mL),  Staphylococcus aureus(MRSA)(MIC=4 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=8 μg/mL), E. coli(MIC=4 μg/mL), Cephalosporin-resistant E. coli(MIC=16 μg/mL).	[Ref.34968054]MHC>128 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 2 and 6) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (2) and Ⓚ (6) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC50=100 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29343	VKRFKⓀFFRⓀFKKFV	VKRFKKFFRKFKKFV	VKRFKKFFRKFKKFV	15	LS-Cathelicidin-BF-15-a1-3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=4μg/mL), Staphylococcus aureus BNCC 186335(MIC=2 μg/mL),  Staphylococcus aureus(MRSA)(MIC=4 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=8 μg/mL), E. coli(MIC=4 μg/mL), Cephalosporin-resistant E. coli(MIC=8 μg/mL).	[Ref.34968054]MHC=32 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 6 and 10) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (6) and Ⓚ (10) are cross-linked by 1,2-bismethylenebenzene via N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC90=128 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29344	VⓀRFKⓀFFRKFKKFV	VKRFKKFFRKFKKFV	VKRFKKFFRKFKKFV	15	LS-Cathelicidin-BF-15-a1-4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=16 μg/mL), Staphylococcus aureus BNCC 186335(MIC=4 μg/mL),  Staphylococcus aureus(MRSA)(MIC=8 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=16 μg/mL), E. coli(MIC=8 μg/mL), Cephalosporin-resistant E. coli(MIC=16 μg/mL).	[Ref.34968054]MHC>128 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 2 and 6) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (2) and Ⓚ (6) are cross-linked by 1,2-bismethylenebenzene via N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC50=128 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29345	VKRFKⓀFFRⓀFKKFV	VKRFKKFFRKFKKFV	VKRFKKFFRKFKKFV	15	LS-Cathelicidin-BF-15-a1-5	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=2 μg/mL), Staphylococcus aureus BNCC 186335(MIC=2 μg/mL),  Staphylococcus aureus(MRSA)(MIC=4 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=16 μg/mL), E. coli(MIC=2 μg/mL), Cephalosporin-resistant E. coli(MIC=16 μg/mL).	[Ref.34968054]MHC>128 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 6 and 10) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (6) and Ⓚ (10) are cross-linked by a but-2-ynyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC90=128 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29346	VⓀRFKⓀFFRKFKKFV	VKRFKKFFRKFKKFV	VKRFKKFFRKFKKFV	15	LS-Cathelicidin-BF-15-a1-6	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.34968054]Gram-positive bacteria:Listeria monocytogenes(MIC=8μg/mL), Staphylococcus aureus BNCC 186335(MIC=4 μg/mL),  Staphylococcus aureus(MRSA)(MIC=8 μg/mL) ;##Gram-negative bacteria:P. aeruginosa(MIC=16 μg/mL), E. coli(MIC=4 μg/mL), Cephalosporin-resistant E. coli(MIC=16 μg/mL).	[Ref.34968054]MHC>128 μg/mL. The MHC is the minimum peptide concentration that caused 10% hemolysis of hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓚ (position: 2 and 6) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. ②Ⓚ (2) and Ⓚ (6) are cross-linked by a but-2-ynyl spacer employing the N-alkylation reaction.	L	[Ref.34968054]Human embryonic kidney HEK293T cells: LC50=100 µg/ml.	34968054	J Med Chem. 2022 Jan 13;65(1):579-591. 	Hu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. 	Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo.	Stapled AMP						
DRAMP29347	FIIIKKSGGLFKKKAGAⓧKKKⓧIKK	FIIIKKSGGLFKKKAGAKKKKKIKK	FIHHIIGGLFSAGKAIHRLIRRRRR	25	TP4-1	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.36877022]Gram-positive bacteria: Staphylococcus aureus(MIC>25 μM; MBC>25 μM);##Gram-negative bacteria:Acinetobacter baumannii(MIC>25 μM; MBC>25 μM).	[Ref.36877022]It shows 15% hemolysis against human red blood cells at the concentration greater than 100 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 18 and 22) in sequence indicates Fmoc-(R)-2-(4-pentenyl) alanine. ②Ⓧ (18) and Ⓧ (22) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	36877022	Microbiol Spectr. 2023 Mar 6;11(2):e0385322.	Yeh JC, Hazam PK, Hsieh CY, Hsu PH, Lin WC, Chen YR, Li CC, Chen JY. 	Rational Design of Stapled Antimicrobial Peptides to Enhance Stability and In Vivo Potency against Polymicrobial Sepsis. 	Stapled AMP						
DRAMP29348	FIIIKKSGGLⓧKKKⓧGAⓧKKKⓧIKK	FIIIKKSGGLKKKKKGAKKKKKIKK	FIHHIIGGLFSAGKAIHRLIRRRRR	25	TP4-2	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.36877022]Gram-positive bacteria: Staphylococcus aureus(MIC>25 μM; MBC>25 μM);##Gram-negative bacteria:Acinetobacter baumannii(MIC=12.5 μM; MBC=12.5 μM).	[Ref.36877022]It shows 15% hemolysis against human red blood cells at the concentration greater than 100 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 11, 15, 18 and 22) in sequence indicates Fmoc-(R)-2-(4-pentenyl) alanine. ②Ⓧ (11) and Ⓧ (15), Ⓧ (18) and Ⓧ (22) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	36877022	Microbiol Spectr. 2023 Mar 6;11(2):e0385322.	Yeh JC, Hazam PK, Hsieh CY, Hsu PH, Lin WC, Chen YR, Li CC, Chen JY. 	Rational Design of Stapled Antimicrobial Peptides to Enhance Stability and In Vivo Potency against Polymicrobial Sepsis. 	Stapled AMP						
DRAMP29349	FIIⓧKKSⓧGLFKKKAGAⓧKKKⓧIKK	FIIKKKSKGLFKKKAGAKKKKKIKK	FIHHIIGGLFSAGKAIHRLIRRRRR	25	TP4-3	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	TP4-3 retained its activity against A. baumannii in the presence of 50% human serum(MIC=3.13 μM; MBC=3.13 μM).	[Ref.36877022]Gram-positive bacteria: Staphylococcus aureus(MIC>25 μM; MBC>25 μM);##Gram-negative bacteria:Acinetobacter baumannii(MIC=3.13 μM; MBC=3.13 μM).	[Ref.36877022]It shows 15% hemolysis against human red blood cells at the concentration greater than 100 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 4, 8, 18 and 22) in sequence indicates Fmoc-(R)-2-(4-pentenyl) alanine.②Ⓧ (4) and Ⓧ (8), Ⓧ (18) and Ⓧ (22) are cross-linked by hydrocarbon stapling respectively.	L	[Ref.36877022]TP4-3 showed <10% cell death at 3.13 μM for HaCaT cells, 3.13 μM for HK-2 cells, and 12.5 μM for RAW 264.7 macrophage cells. 	36877022	Microbiol Spectr. 2023 Mar 6;11(2):e0385322.	Yeh JC, Hazam PK, Hsieh CY, Hsu PH, Lin WC, Chen YR, Li CC, Chen JY. 	Rational Design of Stapled Antimicrobial Peptides to Enhance Stability and In Vivo Potency against Polymicrobial Sepsis. 	Stapled AMP						
DRAMP29350	FIIⓧKKSⓧGLⓧKKKⓧGAⓧKKKⓧIKK	FIIKKKSKGLKKKKKGAKKKKKIKK	FIHHIIGGLFSAGKAIHRLIRRRRR	25	TP4-4	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.	[Ref.36877022]Gram-positive bacteria: Staphylococcus aureus(MIC>25 μM; MBC>25 μM);##Gram-negative bacteria:Acinetobacter baumannii(MIC=12.5 μM; MBC=12.5 μM).	[Ref.36877022]It shows 15% hemolysis against human red blood cells at the concentration greater than 100 μM.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 4, 8, 11, 15, 18 and 22) in sequence indicates Fmoc-(R)-2-(4-pentenyl) alanine. ②Ⓧ (4) and Ⓧ (8), Ⓧ (11) and Ⓧ (15),  Ⓧ (18) and Ⓧ (22) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	36877022	Microbiol Spectr. 2023 Mar 6;11(2):e0385322.	Yeh JC, Hazam PK, Hsieh CY, Hsu PH, Lin WC, Chen YR, Li CC, Chen JY. 	Rational Design of Stapled Antimicrobial Peptides to Enhance Stability and In Vivo Potency against Polymicrobial Sepsis. 	Stapled AMP						
DRAMP29351	ⓧLFDⓧIKKIAESF	XLFDXIKKIAESF	GLFDIIKKIAESF	13	SAU-1	No entry found		Synthetic construct	Antimicrobial, Antifungal		60.2% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC=32 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC>128 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC=128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 1 and 5) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (1) and Ⓧ (5) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides. 	Stapled AMP						
DRAMP29352	GⓧFDIⓧKKIAESF	GXFDIXKKIAESF	GLFDIIKKIAESF	13	SAU-2	No entry found		Synthetic construct	Antimicrobial, Antifungal		52.5% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC=16 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC=128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides. 	Stapled AMP						
DRAMP29353	GLⓧDIIⓧKIAESF	GLXDIIXKIAESF	GLFDIIKKIAESF	13	SAU-3	No entry found		Synthetic construct	Antimicrobial, Antifungal		72.3% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC>128 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 3 and 7) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (3) and Ⓧ (7) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides. 	Stapled AMP						
DRAMP29354	GLFⓧIIKⓧIAESF	GLFXIIKXIAESF	GLFDIIKKIAESF	13	SAU-4	No entry found		Synthetic construct	Antimicrobial, Antifungal		73.5% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC>128 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 4 and 8) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (4) and Ⓧ (8) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides. 	Stapled AMP						
DRAMP29355	GLFDⓧIKKⓧAESF	GLFDXIKKXAESF	GLFDIIKKIAESF	13	SAU-5	No entry found		Synthetic construct	Antimicrobial, Antifungal		61.0% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC=16 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC=16 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 5 and 9) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (5) and Ⓧ (9) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.3 Peptides.	Stapled AMP						
DRAMP29356	GLFDIⓧKKIⓧESF	GLFDIXKKIXESF	GLFDIIKKIAESF	13	SAU-6	No entry found		Synthetic construct	Antimicrobial, Antifungal		49.9% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC>128 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 6 and 10) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides. 	Stapled AMP						
DRAMP29357	GLFDIIⓧKIAⓧSF	GLFDIIXKIAXSF	GLFDIIKKIAESF	13	SAU-7	No entry found		Synthetic construct	Antimicrobial, Antifungal		65.0% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC>128 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 7 and 11) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (7) and Ⓧ (11) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides. 	Stapled AMP						
DRAMP29358	GLFDIIKⓧIAEⓧF	GLFDIIKXIAEXF	GLFDIIKKIAESF	13	SAU-8	No entry found		Synthetic construct	Antimicrobial, Antifungal		83.1% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC>128 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 8 and 12) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (8) and Ⓧ (12) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides. 	Stapled AMP						
DRAMP29359	GLFDIIKKⓧAESⓧ	GLFDIIKKXAESX	GLFDIIKKIAESF	13	SAU-9	No entry found		Synthetic construct	Antimicrobial, Antifungal		67.8% α-helix in a solution of phosphate buffer and trifluoroethanol (7:3) and reached a concentration of 50 μM. 	No other descriptive information about the structure found in the literature	Not available	Function: Antifungal.	[Ref.34439006]Fungi: C. albicans SC5314(MIC>64 μg/mL), C. albicans 901(MIC>128 μg/mL),  C. albicans 904(MIC>128 μg/mL), C. tropicalis ATCC 20026 (MIC>128 μg/mL),  C. tropicalis 895 (MIC=32 μg/mL),  C. glabrata ATCC 1182 (MIC>128 μg/mL),  C. glabrata 896 (MIC>128 μg/mL),  C. auris 918 (MIC>128 μg/mL),  C. auris 919 (MIC>128 μg/mL),  C. krusei ATCC 2340 (MIC>128 μg/mL),  C. parapsilosis ATCC 22010(MIC>128 μg/mL).	No hemolytic activity information found.	Cyclic (Stapled)	Acetylation	Amidation	①The Ⓧ (position: 9 and 13) in sequence indicates S5 (2-amino-2-methylhept-6-enoic acid). ②Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling respectively.	L	No cytotoxicity information found in the reference	34439006	Antibiotics (Basel). 2021 Aug 9;10(8):956. 	Zheng M, Wang R, Chen S, Zou Y, Yan L, Zhao L, Li X.	Design, Synthesis and Antifungal Activity of Stapled Aurein1.4 Peptides.	Stapled AMP						
DRAMP29360	LⓧRRLⓧR	LXRRLXR	LARRLAR	7	stRRL	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		α-helical conformation in an aqueous environment(phosphate buffered saline, PBS), negative electric environment(sodium dodecyl sulfate, SDS), and hydrophobic environment(tri-fluoroethyl alcohol, TFE).	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-negative bacteria.	[Ref.37531494]Gram-negativebacteria:E. coli ATCC25922(MIC=8.00 μM), E. coli UB1005(MIC=4.00 μM), E. coli K99(MIC=8.00 μM), E. coli 987P(MIC= 4.00 μM), S. typhimurium ATCC14028(MIC=32.00 μM), P. aeruginosa PAO1(MIC=16.00 μM).	[Ref.37531494]MHC>256 μM. MHC is the minimum peptide concentration that caused >5% hemolysis of hRBCs. 	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates S-(2,4)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling respectively.	L	[Ref.37531494]<10% cytotoxicity against human embryonic kidney cells (HEK293T) and intestinal porcine enterocyte cells (IPEC-J2) up to 128 μM. 71.50% cell viability against murine macrophage cells (RAW264.7) at 128 μM.	37531494	J Med Chem. 2023 Aug 24;66(16):11414-11427. 	Shao C, Jian Q, Li B, Zhu Y, Yu W, Li Z, Shan A.	Ultrashort All-Hydrocarbon Stapled α-Helix Amphiphile as a Potent and Stable Antimicrobial Compound. 	Stapled AMP						
DRAMP29361	LⓧRLLⓧR	LXRLLXR	LARLLAR	7	stRLL	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-negative bacteria.	[Ref.37531494]Gram-negativebacteria:E. coli ATCC25922(MIC=16.00 μM), E. coli UB1005(MIC=8.00 μM), E. coli K99(MIC=16.00 μM), E. coli 987P(MIC= 8.00 μM), S. typhimurium ATCC14028(MIC=32.00 μM), P. aeruginosa PAO1(MIC=32.00 μM).	[Ref.37531494]MHC=128 μM. MHC is the minimum peptide concentration that caused >5% hemolysis of hRBCs. 8.54% and 29.1% hemolysis at  128 and 256 μM against  hRBCs.	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates S-(2,4)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling respectively.	L	[Ref.37531494]<10% cytotoxicity against human embryonic kidney cells (HEK293T) and intestinal porcine enterocyte cells (IPEC-J2) up to 128 μM. 21.78% cell viability against murine macrophage cells (RAW264.7) at 128 μM.	37531494	J Med Chem. 2023 Aug 24;66(16):11414-11427. 	Shao C, Jian Q, Li B, Zhu Y, Yu W, Li Z, Shan A.	Ultrashort All-Hydrocarbon Stapled α-Helix Amphiphile as a Potent and Stable Antimicrobial Compound. 	Stapled AMP						
DRAMP29362	LⓧLRLⓧR	LXLRLXR	LALRLAR	7	stLRL	No entry found		Synthetic construct	Antimicrobial, Antibacterial, Anti-Gram-		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Function: Antibacterial activity against Gram-negative bacteria.	[Ref.37531494]Gram-negativebacteria:E. coli ATCC25922(MIC=16.00 μM), E. coli UB1005(MIC=16.00 μM), E. coli K99(MIC=16.00 μM), E. coli 987P(MIC=8.00 μM), S. typhimurium ATCC14028(MIC=64.00 μM), P. aeruginosa PAO1(MIC=32.00 μM).	[Ref.37531494]MHC>256 μM. MHC is the minimum peptide concentration that caused >5% hemolysis of hRBCs. 	Cyclic (Stapled)	Free	Amidation	①The Ⓧ (position: 2 and 6) in sequence indicates S-(2,4)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling respectively.	L	[Ref.37531494]<10% cytotoxicity against human embryonic kidney cells (HEK293T) and intestinal porcine enterocyte cells (IPEC-J2) up to 128 μM. 55.18% cell viability against murine macrophage cells (RAW264.7) at 128 μM.	37531494	J Med Chem. 2023 Aug 24;66(16):11414-11427. 	Shao C, Jian Q, Li B, Zhu Y, Yu W, Li Z, Shan A.	Ultrashort All-Hydrocarbon Stapled α-Helix Amphiphile as a Potent and Stable Antimicrobial Compound. 	Stapled AMP						
DRAMP38092	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG 	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	37	RQ-02	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	RQ-01, which exhibits lownanomolar potency across all SARS-CoV-2 strains tested to date.Compared to previously reported HR2-based constructs that weretested in small animals16,20, RQ-01 exhibits markedly improved peptidestability and solubility, enhanced potency and breadth of antiviralactivity, and fully on-resin chemical synthesis, including the lipidationstep, thereby streamlining synthesis and purification for facile itera-tion, lead selection, and upscale. The local tissue persistence of nasallyadministered compound showcases the desirable pharmacologicproperties of stapled lipopeptides, with RQ-01 protecting hamstersfrom SARS-CoV-2-induced weight loss and pulmonary damage	[Ref.38177138]SARS-CoV:IC50=4.5 × 10-8,PV:IC50=1.9 × 10-8 against Wuhan-hu-1 strain,IC50=4.2 × 10-8 against B.1 D614G strain,IC50=2.6 × 10-8 against PV B.1.1.7 strain,IC50=2.4 × 10-8 against PV B.1.135 strain,IC50= against PV 5.3 × 10-9 B.1.1.529.4/5 strain.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is choleaterol with peg length is 8	L	No cytotoxicity information found in the reference(s) presented	38177138	Nature communications, 15(1), 274.	Godes, M., Moyer, B. M., Owen, C. D., DaSilva-Jardine, P., Neuberg, D. S., Bowen, R. A., Davey, R. A., & Walensky, L. D. (2024).	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38093	ⓍDLTⓍEMLSLQQVVKALNESY	DLTAEMLSLQQVVKALNESY	DLTAEMLSLQQVVKALNESY	21	P21S1	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxyamidation	①The Ⓧ (position: 1 and 5) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ(1) and Ⓧ (5) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38094	LⓍLTYⓍMLSLQQVVKALNESY	ALTAAMLSLQQVVKALNESY	ALTAAMLSLQQVVKALNESY	21	P21S2	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.90 ± 1.1 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 2 and 6) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38095	LDLⓍYEMⓍSLQQVVKALNESY	DLAYEMASLQQVVKALNESY	DLAYEMASLQQVVKALNESY	21	P21S3	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 4 and 8) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (4) and Ⓧ (8) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38096	LDLTⓍEMLⓍLQQVVKALNESY	DLTAEMALQQVVKALNESY	DLTAEMALQQVVKALNESY	21	P21S4	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=7.14 ± 0.7 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 5 and 9) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (5) and Ⓧ (9) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38097	LDLTYEMⓍSLQⓍVVKALNESY	DLTYEMASLAVVKALNESY	DLTYEMASLAVVKALNESY	21	P21S5	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=10.7±2.6 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 8 and 12) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (8) and Ⓧ (12) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38098	LDLTYEMLⓍLQQⓍVKALNESY	DLTYEMALQQAVKALNESY	DLTYEMALQQAVKALNESY	21	P21S6	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 9 and 13) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (9) and Ⓧ (13) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38099	LDLTYEMLSLⓍQVVⓍALNESY	DLTYEMASLQAVVKALNESY	DLTYEMASLQAVVKALNESY	21	P21S7	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50>50 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 11 and 15) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (11) and Ⓧ (15) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38100	LDLTYEMLSLQⓍVVKⓍLNESY	DLTYEMASLQQVVKALNESY	DLTYEMASLQQVVKALNESY	21	P21S8	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.26±0.05 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=3.03 ± 0.29 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=4.06± 0.34 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.98± 0.28 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (12) and Ⓧ (16) are cross-linked by hydrocarbon stapling.	L	[Ref.29442512]Calu-3 cell:CC50>100 μM	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38101	LDLTYEMLSLQQVVⓍALNⓍSY	DLTYEMASLQQVVKALNESY	DLTYEMASLQQVVKALNESY	21	P21S9	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=14.1 ± 2.3 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxamidation	①The Ⓧ (position: 15 and 19) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (15) and Ⓧ (19) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38102	LDLTYEMLSLQQVVKⓍLNEⓍY	DLTYEMASLQQVVKALNESY	DLTYEMASLQQVVKALNESY	21	P21S10	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.33 ± 0.04 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.97± 0.08 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=1.82± 0.28 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=0.89± 0.07 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxyamidation	①The Ⓧ (position: 16 and 20) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (16) and Ⓧ (20) are cross-linked by hydrocarbon stapling.	L	[Ref.29442512]Calu-3 cell:CC50>100 μM	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38103	LDLTYEMLSLQⓍVVKⓍLNESY	DLTYEMASLQAVVKALNESY	DLTYEMASLQAVVKALNESY	21	P21R8	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=16.3 ± 1.1 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxyamidation	①The Ⓧ at position 12 and 16 are R5 amino acids. ②Ⓧ (12) and Ⓧ (16) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38104	LDLTYEⓏLSLQⓍVVKⓍLNESY	DLTYEZLSLQAVVKALNESY	DLTYEZLSLQAVVKALNESY	21	P21S8Z	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=0.63 ± 0.05 μM);##WT MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=2.80 ± 0.74 μM);##Q1020H-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=4.15± 0.25 μM);##Q1020R-MERS-CoV pseudovirus:inhibition of pseudovirus infection in calu-3 cells(EC50=2.49±0.18 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxyamidation	①The Ⓧ (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (12) and Ⓧ (16) are cross-linked by hydrocarbon stapling. The Ⓩ at position 7 indicates R8 ((R)-octenyl alanine)	L	[Ref.29442512]Calu-3 cell:CC50>100 μM	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38105	LDLTYEMLSLQⓍVVKⓍLNESF	DLTYEMASLQAVVKALNESF	DLTYEMASLQAVVKALNESF	21	P21S8F	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=2.16± 1.1 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxyamidation	①The Ⓧ (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (12) and Ⓧ (16) are cross-linked by hydrocarbon stapling.	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38106	LDLTYEⓏLSLQⓍVVKⓍLNESF	DLTYEZLSLQAVVKALNESF	DLTYEZLSLQAVVKALNESF	21	P21S8ZF	Not Available	Coronaviridae	Synthetic construct (From S2 unit of MERS-Cov)		Not Available	Not Available	Not Available	Not Available	The peptide inhibits MERS-CoV infection and its spike (S) protein-mediated cell–cell fusion.	[Ref.29442512]MERS-CoV:inhibition of cell-cell fusion in Huh-7 cells(EC50=3.89 ± 0.8 μM).	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Carboxyamidation	①The Ⓧ (position: 12 and 16) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②Ⓧ (12) and Ⓧ (16) are cross-linked by hydrocarbon stapling.,The Ⓩ at position 7 indicates R8 ((R)-octenyl alanine)	L	No cytotoxicity information found in the reference(s) presented	29442512	Journal of medicinal chemistry, 61(5), 2018–2026.	Wang, C., Xia, S., Zhang, P., Zhang, T., Wang, W., Tian, Y., Meng, G., Jiang, S., & Liu, K. (2018).	Discovery of Hydrocarbon-Stapled Short α-Helical Peptides as Promising Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Fusion Inhibitors	Stapled AMP						
DRAMP38107	ISF c'ELLDYYC'ESGS 	ISFCELLDYYCESGS	ISFCELLDYYCESGS	14	1	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.	[Ref:24613163]HIV:IC50=2.8 ± 0.2μM in MT-2 cells, IC50=1.9 ± 0.2μM in TZM-b1 cells.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	c' and C' denote the Bph-linked D-cysteine and L-cysteine, respectively.	L	[Ref:24613163]HIV:CC50=>103µM in MT-2 cells,CC50=>103µM in TZM b1 cells	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38108	ISF c'QLLDYYC'ESGS 	ISFCQLLDYYCESGS	ISFCQLLDYYCESGS	14	2	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.	[Ref:24613163]HIV:IC50=5.5 ± 1.4μM in MT-2 cells, IC50=3.1 ± 0.3μM in TZM-b1 cells.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	c' and C' denote the Bph-linked D-cysteine and L-cysteine, respectively.	L	[Ref:24613163]HIV:CC50=>103µM in MT-2 cells,CC50=>103µM in TZM b1 cells	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38109	ISF c'ELLNYYC'ESGS 	ISFCELLNYYCESGS	ISFCELLNYYCESGS	14	3	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.	[Ref:24613163]HIV:IC50=8.8 ± 0.5μM in MT-2 cells, IC50=1.8 ± 0.1μM in TZM-b1 cells.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	c' and C' denote the Bph-linked D-cysteine and L-cysteine, respectively.	L	[Ref:24613163]HIV:CC50=>102µM in MT-2 cells,CC50=>102µM in TZM b1 cells	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38110	ISF c'QLLNYYC'ESGS 	ISFCQLLNYYCESGS	ISFCQLLNYYCESGS	14	4	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.	[Ref:24613163]HIV:IC50=5.7 ± 0.1μM in MT-2 cells, IC50=1.6 ± 0.2μM in TZM-b1 cells.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	c' and C' denote the Bph-linked D-cysteine and L-cysteine, respectively.	L	[Ref:24613163]HIV:CC50=~51µM in MT-2 cells,CC50=>102µM in TZM b1 cells	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38111	ISF c'ELADYYC'ESGS 	ISFCELADYYCESGS	ISFCELADYYCESGS	14	5	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.	[Ref:24613163]HIV:IC50=4.1 ± 0.3μM in MT-2 cells, IC50=1.4 ± 0.2μM in TZM-b1 cells.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	c' and C' denote the Bph-linked D-cysteine and L-cysteine, respectively.	L	[Ref:24613163]HIV:CC50=~26µM in MT-2 cells,CC50=>52µM in TZM b1 cells	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38112	ISF c'ELLDYAC'ESGS 	ISFCELLDYACESGS	ISFCELLDYACESGS	14	6	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.	[Ref:24613163]HIV:IC50=14.0 ± 1.1μM in MT-2 cells, IC50=17.3 ± 1.4μM in TZM-b1 cells.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	c' and C' denote the Bph-linked D-cysteine and L-cysteine, respectively.	L	[Ref:24613163]HIV:CC50=>107µM in MT-2 cells,CC50=>107µM in TZM b1 cells	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38113	Fluorescein-Ahx- ISF c'ELLDYYC'ESGS 	ISFCELLDYYCESGS	ISFCELLDYYCESGS	14	FITC-1 	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.	No MIC Avaiable in the. Reference	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	c′ and C′ denote Bph-linked D-cysteine and L-cysteine, respectively.	L	No cytotoxicity information found in the reference(s) presented	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38114	ISFⓇELLDYYⓈESGSc	ISFRELLDYYSESGSC	ISFRELLDYYSESGSC	16	NYAD-36	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:24613163]HIV:IC50=1.5 ± 0.17μM in MT-2 cells, IC50=2.0 ± 0.4μM in TZM-b1 cells.	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Free	Free	Hydrocarbon stapling occurs between Ⓡ and Ⓢ: R8 = (R)-2-(7′-octenyl)alanine; S5 = (S)-2-(4′-pentenyl)alanine.	L	[Ref:24613163]HIV:CC50=>1189.4µM in MT-2 cells,CC50=>189.4µM in TZM b1 cells	24613163	Bioorg Med Chem Lett. 2014 Apr 1;24(7):1748-51.	Muppidi A, Zhang H, Curreli F, Li N, Debnath AK, Lin Q.	Design of antiviral stapled peptides containing a biphenyl cross-linker	Stapled AMP						
DRAMP38115	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEGO-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=1.2 × 10-7 in  B.1.1.529.1 strain,SARS-CoV:IC50=1.6 × 10-6,LV:IC50=5.0 x 10-6 against Beta strain((B.1.351))	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 0	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38116	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	 SAH-HR2-D-PEG3-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=3.3 × 10⁻⁷ in B.1.1.529.1 strain, SARS-CoV:IC50=1.3 × 10⁻⁶, LV:IC50=5.2 × 10⁻⁶ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 3	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38117	DISGINASVVNIQEIDRLNⓍVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG4-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=3.6 × 10⁻⁸ in B.1.1.529.1 strain, SARS-CoV:IC50=1.5 × 10⁻⁷, LV:IC50=5.6 × 10⁻⁷ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 4	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38118	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG5-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=3.1 × 10⁻⁸ in B.1.1.529.1 strain, SARS-CoV:IC50=2.8 × 10⁻⁷, LV:IC50=1.3 × 10⁻⁶ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 5	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38119	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG6-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=9.0 × 10⁻⁸ in B.1.1.529.1 strain, SARS-CoV:IC50=2.4 × 10⁷, LV:IC50=6.5 × 10⁻⁷ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 6	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38120	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG7-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=5.2 × 10⁻⁸ in B.1.1.529.1 strain, SARS-CoV:IC50=2.4 × 10⁻⁷, LV:IC50=7.0 × 10⁻⁷ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 7	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38121	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG8-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=3.0 × 10⁻⁹ in B.1.1.529.1 strain, SARS-CoV:IC50=6.5 × 10⁻⁸, LV:IC50=2.2 × 10⁻⁷ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 8	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38122	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG10-TC 	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=3.3 × 10⁻⁸ in B.1.1.529.1 strain, SARS-CoV:IC50=9.6 × 10⁻⁸, LV:IC50=1.3 × 10⁻⁷ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 10	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38123	DISGINASVVNIKEIDRLⓍEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG12-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=4.2 × 10⁻⁹ in B.1.1.529.1 strain, SARS-CoV:IC50=8.0 × 10⁻⁸, LV:IC50=1.7 × 10⁻⁷ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is Ⓧ and it is tricholeaterol with peg length is 12	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38124	DISGINASVVNI8KEIDRLXEVAKNLNESLIDLQELG(K*)	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG14-TC 	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=7.8 × 10⁻⁹ in B.1.1.529.1 strain, SARS-CoV:IC50=4.7 × 10⁻⁸, LV:IC50=1.7 × 10⁻⁷ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is D and it is tricholeaterol with peg length is 14	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38125	DISGINASVVNI8KEIDRLXEVAKNLNESLIDLQELG(K*) 	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG16-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=3.0 × 10⁻⁹ in B.1.1.529.1 strain, SARS-CoV:IC50=2.3 × 10⁻⁸, LV:IC50=9.0 × 10⁻⁸ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is D and it is tricholeaterol with peg length is 16	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP38126	DISGINASVVNI8KEIDRLXEVAKNLNESLIDLQELG(K*)	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	DISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELG	38	SAH-HR2-D-PEG20-TC	Not Available	Coronaviridae	Synthetic Construct		Not Available	Not Available	Not Available	Not Available	Not Available	[Ref:38177138]PV:IC50=4.3 × 10⁻⁹ in B.1.1.529.1 strain, SARS-CoV:IC50=2.3 × 10⁻⁸, LV:IC50=7.2 × 10⁻⁸ against Beta strain (B.1.351)	No hemolysis information or data found in the reference(s) presented in this entry	Cyclic (Stapled)	Acetylation	Free	Staple location is D and it is tricholeaterol with peg length is 20	L	No cytotoxicity information found in the reference(s) presented	38177138	Nat Commun. 2024 Jan 4;15(1):274.	Bird GH, Patten JJ, Zavadoski W, Barucci N, Godes M, Moyer BM, Owen CD, DaSilva-Jardine P, Neuberg DS, Bowen RA, Davey RA, Walensky LD.	A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential	Stapled AMP						
DRAMP32456	GIMⓍSLMⓍKLAAHIAK	GIMXSLMXKLAAHIAK		16	HYL-18	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 (IC50=1.48±0.15 µmol/L); A549 (IC50=2.38±0.38 µmol/L); Hep-G2 (IC50=2.67±0.29 µmol/L)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL	Not available	Not available	Not available	Structural modification and antitumor activity of antimicrobial peptide HYL	Stapled AMP						
DRAMP32458	GIMSⓍLMKⓍLAAHIAK	GIMSXLMKXLAAHIAK		16	HYL-17	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 (IC50=1.54±0.32 µmol/L); A549 (IC50=5.56±0.41 µmol/L); Hep-G2 (IC50=9.70±0.50 µmol/L)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(5) and Ⓧ (9) are cross-linked by hydrocarbon stapling	L	Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL	Not available	Not available	Not available	Structural modification and antitumor activity of antimicrobial peptide HYL	Stapled AMP						
DRAMP32462	GIMSSLMⓍKLAⓍHIAK	GIMSSLMXKLAXHIAK		16	HYL-16	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 (IC50=1.90±0.35 µmol/L); A549 (IC50=2.36±0.23 µmol/L); Hep-G2 (IC50=2.45±0.22 µmol/L)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(8) and Ⓧ (12) are cross-linked by hydrocarbon stapling	L	Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL	Not available	Not available	Not available	Structural modification and antitumor activity of antimicrobial peptide HYL	Stapled AMP						
DRAMP32464	GIMSSLMKⓍLAAⓍIAK	GIMSSLMKXLAAXIAK		16	HYL-15	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 (IC50=2.52±0.42 µmol/L); A549 (IC50=3.17±0.33 µmol/L); Hep-G2 (IC50=3.38±0.26 µmol/L)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(9) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL	Not available	Not available	Not available	Structural modification and antitumor activity of antimicrobial peptide HYL	Stapled AMP						
DRAMP32467	GIMSSLMKKLⓍAHIⓍK	GIMSSLMKKLXAHIXK		16	HYL-14	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: A549 (IC50=1.36±0.35 µmol/L); HCT 116 (IC50=1.61±0.27 µmol/L); Hep-G2 (IC50=1.67±0.25 µmol/L)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(11) and Ⓧ (15) are cross-linked by hydrocarbon stapling	L	Human Splenic Fibroblasts (HSF): IC50=12.78±0.33 µg/mL; Endometrial epithelial cells(HEEC): IC50=2.66±0.34 µg/mL; HPDE6c7 Human Pancreatic Duct Epithelial Cell: IC50=3.45±0.20 µg/mL; Normal Human Hepatic Cell (Lo-2): IC50=2.91±0.07 µg/mL; NCM460: IC50=3.04±0.10 µg/mL; CCD-19Lu: IC50=4.76±0.03 µg/mL	Not available	Not available	Not available	Structural modification and antitumor activity of antimicrobial peptide HYL	Stapled AMP						
DRAMP32481	TAWYANFⓍKLLⓍ	TAWYANFXKLLX		12	DPMI-δ-F	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Not available	Not available	Stapled: Ⓧ(8) and Ⓧ (12) are cross-linked by hydrocarbon stapling	L	Not available	Not available	Not available	Not available	Not available	Stapled AMP						
DRAMP32482	TAWYⓍNFEⓍLLR	TAWYXNFEXLLR		12	DPMI-δ-D	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Not available	Not available	Stapled: Ⓧ(5) and Ⓧ (9) are cross-linked by hydrocarbon stapling	L	Not available	Not available	Not available	Not available	Not available	Stapled AMP						
DRAMP32483	TAWYⓍNFEKLLⓍ	TAWYXNFEKLLX		12	DPMI-δ-B	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Not available	Not available	Stapled: Ⓧ(5) and Ⓧ (12) are cross-linked by hydrocarbon stapling	L	Not available	Not available	Not available	Not available	Not available	Stapled AMP						
DRAMP32484	WYANFⓍKLLⓍ	WYANFXKLLX		10	DPMI-δ-E	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Not available	Not available	Stapled: Ⓧ(6) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	Not available	Not available	Not available	Not available	Stapled AMP						
DRAMP32485	WYⓍNFEⓍLLR	WYXNFEXLLR		10	DPMI-δ-C	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Not available	Not available	Stapled: Ⓧ(3) and Ⓧ (7) are cross-linked by hydrocarbon stapling	L	Not available	Not available	Not available	Not available	Not available	Stapled AMP						
DRAMP32486	WYⓍNFEKLLⓍ	WYXNFEKLLX		10	DPMI-δ-A	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Not available	Not available	Stapled: Ⓧ(3) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	Not available	Not available	Not available	Not available	Stapled AMP						
DRAMP33751	IKLSKETKKNLKKVLKGAIKGⓍIAVⓍKMV	IKLSKETKKNLKKVLKGAIKGXIAVXKMV	IKLSKETKKNLKKVLKGAIKGSIAVSKMV	29	H-19, Hymenochirin-1B [P5K,D9K; A18,A22 S5]	W8PRC4		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: A549 (IC50=1.00±0.36 μM); HepG2 (IC50=1.64±0.36 μM); HCT 116 (IC50=1.78±0.35  μM)	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(18) and Ⓧ (22) are cross-linked by hydrocarbon stapling	L	Not available	30789695	ACS Chem Biol. 2019 Mar 15;14(3):516-525. 	Li Y, Zhang Y, Wu M, Chang Q, Hu H, Zhao X.	Improving Selectivity, Proteolytic Stability, and Antitumor Activity of Hymenochirin-1B: A Novel Glycosylated Staple Strategy	Stapled AMP						
DRAMP34558	GLFAVⓍKKVASVⓍKGL	GLFAVXKKVASVXKGL	GLFAVCKKVASVCKG	16	AC-CCSP-5-Dp	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=12.1 μM); U87 (IC50=14.72 μM); A549 (IC50=16.37 μM); C4-2B (IC50=35.84 μM)	Not available	Cyclic (Stapled)	Acetylization	Amidation	Stapled: Ⓧ(6) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Not available	37804993	Bioorg Med Chem Lett. 2023 Nov 15;96:129499.	Shen H, Zhang N, Kong X, Wang N, Hu HG, Cong W, Liu C. 	Benzyl stapled modification and anticancer activity of antimicrobial peptide A4K14-Citropin 1.1	Stapled AMP						
DRAMP34559	GLFAVⓍKKVASVⓍKGL	GLFAVXKKVASVXKGL	GLFAVCKKVASVCKG	16	AC-CCSP-5-Dp	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 (IC50=7.44µM); MCF-7 (IC50=7.47µM); U-87MG ATCC (IC50=9.2µM)	Not available	Cyclic (Stapled)	Acetylization	Amidation	Stapled: Ⓧ(6) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Not available	37804993	Bioorg Med Chem Lett. 2023 Nov 15;96:129499.	Shen H, Zhang N, Kong X, Wang N, Hu HG, Cong W, Liu C. 	Benzyl stapled modification and anticancer activity of antimicrobial peptide A4K14-Citropin 1.1	Stapled AMP						
DRAMP34929	LSQETFSDⓍWKLLPEⓍ	LSQETFSDXWKLLPEX	LSQETFSDWKLLPE	16	SAH-p53-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(9) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-7. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34930	LSQEⓍFSDLWKⓍLPEN	LSQEXFSDLWKXLPEN	LSQEFSDLWKLPEN	16	SAH-p53-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(5) and Ⓧ (12) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-8. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34931	LSQⓍTFSDLWKLLⓍEN	LSQXTFSDLWKLLXEN	LSQTFSDLWKLLEN	16	SAH-p53-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(4) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-9. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34932	LSQETFⓍDLWKLLⓍEN	LSQETFXDLWKLLXEN	LSQETFDLWKLLEN	16	SAH-p53-4	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-10. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34933	LSQETFⓍNLWKLLⓍQN	LSQETFXNLWKLLXQN	LSQETFNLWKLLQN	16	SAH-p53-5	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-11. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34934	LSQQTFⓍNLWRLLⓍQN	LSQQTFXNLWRLLXQN	LSQQTFNLWRLLQN	16	SAH-p53-6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-12. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34935	QSQQTFⓍNLWKLLⓍQN	QSQQTFXNLWKLLXQN	QSQQTFNLWKLLQN	16	SAH-p53-7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-13. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34936	QSQQTFⓍNLWRLLⓍQN	QSQQTFXNLWRLLXQN	QSQQTFNLWRLLQN	16	SAH-p53-8	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-14. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP34937	QSQQTFⓍNLWRLLⓍQN	QSQQTFXNLWRLLXQN	QSQQTFNLWRLLQN	16	SAH-p53-8	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Free	Free	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	22148351	J Am Chem Soc. 2012 Jan 11;134(1):103-14. 	Baek S, Kutchukian PS, Verdine GL, Huber R, Holak TA, Lee KW, Popowicz GM.	Structure of the stapled p53 peptide bound to Mdm2	Stapled AMP						
DRAMP35008	BENPEⓍILDEHVⓍRVM	BENPEXILDEHVXRVM	BENPERILDEHVSRVM	16	fStAx-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(6) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-8.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35009	BENPESILDⓍHVQⓍVM	BENPESILDXHVQXVM	BENPESILDSHVQSVM	16	fStAx-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(10) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-9.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35010	BENPEⓍILDⓍHVQRVM	BENPEXILDXHVQRVM	BENPESILDSHVQRVM	16	fStAx-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(6) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-10.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35011	BPEⓍILDⓍHVQRVM	BPEXILDXHVQRVM	BPESILDSHVQRVM	14	fStAx-31	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-11.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35012	XPQⓍILDⓍHVRRVMR	XPQXILDXHVRRVMR	XPQSILDSHVRRVMR	15	fStAx-32	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-12.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35013	XPQⓍILDⓍHVRRVWR	XPQXILDXHVRRVWR	XPQSILDSHVRRVWR	15	fStAx-33	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-13.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35014	XRWPQⓍILDⓍHVRRVWR	XRWPQXILDXHVRRVWR	XRWPQSILDSHVRRVWR	17	fStAx-34	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(6) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-14.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35015	XRRWPQⓍILDⓍHVRRVWR	XRRWPQXILDXHVRRVWR	XRRWPQSILDSHVRRVWR	18	fStAx-35	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-15.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35016	XRRWPRⓍILDⓍHVRRVWR	XRRWPRXILDXHVRRVWR	XRRWPRSILDSHVRRVWR	18	fStAx-35R	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-16.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35017	XRRWPQⓍILHⓍDVRRVWR	XRRWPQXILHXDVRRVWR	XRRWPQSILHSDVRRVWR	18	fStAx-40	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-17.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35018	XRRWPQⓍILHⓍDVRRVAR	XRRWPQXILHXDVRRVAR	XRRWPQSILHSDVRRVAR	18	fStAx-41	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC	Amidation	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-18.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35019	XRRWPRⓍILHⓍDVRRVAR	XRRWPRXILHXDVRRVAR	XRRWPRSILHSDVRRVAR	18	fStAx-41R	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	FITC		Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-19.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35020	RRWPQⓍILDⓍHVRRVWR	RRWPQXILDXHVRRVWR	RRWPQSILDSHVRRVWR	17	aStAx-35	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(6) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-20.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35021	RRWPRⓍILHⓍDVRRVAR	RRWPRXILHXDVRRVAR	XRRWPRSILHSDVRRVAR	17	aStAx-41R	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(6) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	23071338	 Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17942-21.	Grossmann TN, Yeh JT, Bowman BR, Chu Q, Moellering RE, Verdine GL.	Inhibition of oncogenic Wnt signaling through direct targeting of β-catenin	Stapled AMP						
DRAMP35127	QSQQTFⓍNLWRLLⓍQN	QSQQTFXNLWRLLXQN	QSQQTFRNLWRLLSQN	16	ATSP-1800	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	23946421	Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-54.	Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK.	Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy	Stapled AMP						
DRAMP35128	QSQQTFⓍNLWRLLⓍQN	QSQQTFXNLWRLLXQN	QSQQTFRNLWRLLSQN	16	ATSP-1800	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	23946421	Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-54.	Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK.	Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy	Stapled AMP						
DRAMP35131	LTFⓍHYWAQLⓍS	LTFXHYWAQLXS	LTFRHYWAQLSS	12	ATSP-3900	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23946421	Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-56.	Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK.	Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy	Stapled AMP						
DRAMP35132	LTFⓍAYWAQLⓍS	LTFXAYWAQLXS	LTFRAYWAQLSS	12	ATSP-4641	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23946421	Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-57.	Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK.	Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy	Stapled AMP						
DRAMP35133	LTFⓍEYWAQLⓍS	LTFXEYWAQLXS	LTFREYWAQLSS	12	ATSP-6935	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23946421	Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-58.	Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK.	Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy	Stapled AMP						
DRAMP35134	LTFⓍEYWAQXⓍSAA	LTFXEYWAQXXSAA	LTFREYWAQXSSAA	14	ATSP-7041	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23946421	Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-59.	Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK.	Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy	Stapled AMP						
DRAMP35135	LTAⓍEYWAQXⓍSAA	LTAXEYWAQXXSAA	LTAREYWAQXSSAA	14	ATSP-7342	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	23946421	Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):E3445-60.	Chang YS, Graves B, Guerlavais V, Tovar C, Packman K, To KH, Olson KA, Kesavan K, Gangurde P, Mukherjee A, Baker T, Darlak K, Elkin C, Filipovic Z, Qureshi FZ, Cai H, Berry P, Feyfant E, Shi XE, Horstick J, Annis DA, Manning AM, Fotouhi N, Nash H, Vassilev LT, Sawyer TK.	Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy	Stapled AMP						
DRAMP35158	ISFⓍELLDYYⓍESGS	ISFXELLDYYXESGS	ISFRELLDYYSESGS	15	NYAD-36	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	24237936	Retrovirology. 2013 Nov 15;10:136.	Zhang H, Curreli F, Waheed AA, Mercredi PY, Mehta M, Bhargava P, Scacalossi D, Tong X, Lee S, Cooper A, Summers MF, Freed EO, Debnath AK. 	Not available	Stapled AMP						
DRAMP35159	ISFⓍELLDYYⓍED	ISFXELLDYYXED	ISFRELLDYYSED	13	NYAD-66	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	24237936	Retrovirology. 2013 Nov 15;10:137.	Zhang H, Curreli F, Waheed AA, Mercredi PY, Mehta M, Bhargava P, Scacalossi D, Tong X, Lee S, Cooper A, Summers MF, Freed EO, Debnath AK. 	Not available	Stapled AMP						
DRAMP35160	ISFⓍEWLQAYⓍEDE	ISFXEWLQAYXEDE	ISFREWLQAYSEDE	14	NYAD-67	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	24237936	Retrovirology. 2013 Nov 15;10:138.	Zhang H, Curreli F, Waheed AA, Mercredi PY, Mehta M, Bhargava P, Scacalossi D, Tong X, Lee S, Cooper A, Summers MF, Freed EO, Debnath AK. 	Not available	Stapled AMP						
DRAMP35549	DDEⓍEQFⓍYHLLXFNAV	DDEXEQFXYHLLXFNAV	DDESEQFSYHLLXFNAV	17	StRIP4	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-85. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35550	DDEⓍEQFⓍYHLXSFNAV	DDEXEQFXYHLXSFNAV	DDESEQFSYHLXSFNAV	17	StRIP5	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-86. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35551	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-87. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35552	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-87. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35553	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-87. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35554	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-87. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35555	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-87. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35556	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-88. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35557	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-88. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35558	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-88. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35559	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-88. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35560	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-88. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35561	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP8	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-89. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35562	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP8	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-89. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35563	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP8	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-89. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35564	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP8	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-89. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35565	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP8	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-89. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35566	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP9	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-90. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35567	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP9	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-90. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35568	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP9	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-90. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35569	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP9	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-90. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35570	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP9	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-90. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35571	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP10	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-91. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35572	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP10	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-91. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35573	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP10	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-91. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35574	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP10	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-91. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35575	DDEⓍEQFⓍYHLXSFNXV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLXSFNXV	17	StRIP10	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-91. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35576	DDEⓍEQFLYHⓍLSFNAV	DDEXEQFLYHXLSFNAV	DDEREQFLYHSLSFNAV	17	StRIP11	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-92. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35577	DDEⓍEQFⓍYHLⓍSFNⓍV	DDEXEQFXYHLXSFNXV	DDESEQFSYHLSSFNSV	17	StRIP12	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-93. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35578	DDEⓍEWFⓍYHLⓍSFNⓍV	DDEXEWFXYHLXSFNXV	DDESEWFSYHLSSFNSV	17	StRIP13	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-94. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35579	DDEⓍEWFⓍYHLⓍFFNⓍV	DDEXEWFXYHLXFFNXV	DDESEWFSYHLSFFNSV	17	StRIP14	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-95. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35580	DDEⓍQWFⓍYHLⓍFFNⓍV	DDEXQWFXYHLXFFNXV	DDESQWFSYHLSFFNSV	17	StRIP15	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-96. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35581	DNEⓍQWFⓍYHLⓍFFNⓍV	DNEXQWFXYHLXFFNXV	DNESQWFSYHLSFFNSV	17	StRIP16	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-97. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35582	NDEⓍQWFⓍYHLⓍFFNⓍV	NDEXQWFXYHLXFFNXV	NDESQWFSYHLSFFNSV	17	StRIP17	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-98. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35583	DDEⓍEFFⓍYHLLSFNAV	DDEXEFFXYHLLSFNAV	DDESEFFSYHLLSFNAV	17	StRIP3[Q905F]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-99. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35584	DDEⓍELFⓍYHLLSFNAV	DDEXELFXYHLLSFNAV	DDESELFSYHLLSFNAV	17	StRIP3[Q905L]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-100. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35585	DDEⓍEWFⓍYHLLSFNAV	DDEXEWFXYHLLSFNAV	DDESEWFSYHLLSFNAV	17	StRIP3[Q905W]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-101. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35586	DDEⓍEQFⓍYHLFFFNAV	DDEXEQFXYHLFFFNAV	DDESEQFSYHLFFFNAV	17	StRIP3[L911F,S912F]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-102. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35587	DDEⓍEQFⓍYHLFWFNAV	DDEXEQFXYHLFWFNAV	DDESEQFSYHLFWFNAV	17	StRIP3[L911F,S912W]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-103. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35588	DDEⓍEQFⓍYHLFYFNAV	DDEXEQFXYHLFYFNAV	DDESEQFSYHLFYFNAV	17	StRIP3[L911F,S912Y]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-104. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35589	DDQⓍEWFⓍYHLⓍFFNⓍV	DDQXEWFXYHLXFFNXV	DDQSEWFSYHLSFFNSV	17	StRIP14[E902Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-105. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35590	DNEⓍEWFⓍYHLⓍFFNⓍV	DNEXEWFXYHLXFFNXV	DNESEWFSYHLSFFNSV	17	StRIP14[D901N]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-106. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35591	NDEⓍEWFⓍYHLⓍFFNⓍV	NDEXEWFXYHLXFFNXV	NDESEWFSYHLSFFNSV	17	StRIP14[D900N]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-107. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35592	DNQⓍEWFⓍYHLⓍFFNⓍV	DNQXEWFXYHLXFFNXV	DNQSEWFSYHLSFFNSV	17	StRIP14[D901N,E902Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-108. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35593	NDQⓍEWFⓍYHLⓍFFNⓍV	NDQXEWFXYHLXFFNXV	NDQSEWFSYHLSFFNSV	17	StRIP14[D900N,E902Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-109. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35594	NNEⓍEWFⓍYHLⓍFFNⓍV	NNEXEWFXYHLXFFNXV	NNESEWFSYHLSFFNSV	17	StRIP14[D900N,D901N]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-110. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35595	NNQⓍEWFⓍYHLⓍFFNⓍV	NNQXEWFXYHLXFFNXV	NNQSEWFSYHLSFFNSV	17	StRIP14[D900N,D901N,E902Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-111. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35596	DDQⓍQWFⓍYHLⓍFFNⓍV	DDQXQWFXYHLXFFNXV	DDQSQWFSYHLSFFNSV	17	StRIP14[E902Q,E904Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-112. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35597	DNQⓍQWFⓍYHLⓍFFNⓍV	DNQXQWFXYHLXFFNXV	DNQSQWFSYHLSFFNSV	17	StRIP14[D901N,E902Q,E904Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-113. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35598	NDQⓍQWFⓍYHLⓍFFNⓍV	NDQXQWFXYHLXFFNXV	NDQSQWFSYHLSFFNSV	17	StRIP14[D900N,E902Q,E904Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-114. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35599	NNEⓍQWFⓍYHLⓍFFNⓍV	NNEXQWFXYHLXFFNXV	NNESQWFSYHLSFFNSV	17	StRIP14[D900N,D901N,E904Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-115. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35600	NNQⓍQWFⓍYHLⓍFFNⓍV	NNQXQWFXYHLXFFNXV	NNQSQWFSYHLSFFNSV	17	StRIP14[D900N,D901N,E902Q,E904Q]	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Binds Rab8a(GppNHp) and is able to inhibit a Rab8a PPI.		Not available	Cyclic (Stapled)	Fluorescein-O2OC-	Free	Stapled: Ⓧ(4) and Ⓧ (8), Ⓧ(12) and Ⓧ (16) are cross-linked by hydrocarbon stapling	L	Not available	27336832	ACS Chem Biol. 2016 Aug 19;11(8):2375-116. 	Cromm PM, Spiegel J, Küchler P, Dietrich L, Kriegesmann J, Wendt M, Goody RS, Waldmann H, Grossmann TN.	Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase	Stapled AMP						
DRAMP35711	ALPISTVRⓍVALⓍRRL	ALPISTVRXVALXRRL	ALPISTVRSVALSRRL	16	P2shortA	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: A549 (50% Killing=10 μM); PC-9 (80% Killing=10 μM); NCI-H358 (98% Killing=10 μM)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(9) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Not available	32104498	Theranostics. 2020 Jan 12;10(5):2008-2028. 	Bouclier C, Simon M, Laconde G, Pellerano M, Diot S, Lantuejoul S, Busser B, Vanwonterghem L, Vollaire J, Josserand V, Legrand B, Coll JL, Amblard M, Hurbin A, Morris MC. 	Stapled peptide targeting the CDK4/Cyclin D interface combined with Abemaciclib inhibits KRAS mutant lung cancer growth	Stapled AMP						
DRAMP35725	PQⓍILDQHVⓍRVMK	PQRXILDQHVXRVMK	PQRILDQHVSRVMK	15	SAHPA1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(3) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	32550000	Cell Discov. 2020 Jun 9;6:35.	Liao H, Li X, Zhao L, Wang Y, Wang X, Wu Y, Zhou X, Fu W, Liu L, Hu HG, Chen YG. 	A PROTAC peptide induces durable β-catenin degradation and suppresses Wnt-dependent intestinal cancer	Stapled AMP						
DRAMP35726	PQⓍILDQHVⓍRVMKXALAPYIP	PQRXILDQHVXRVMKXALAPYIP	PQRILDQHVSRVMKXALAPYIP	23	SAHPA1-VHLL	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(3) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	32550000	Cell Discov. 2020 Jun 9;6:36.	Liao H, Li X, Zhao L, Wang Y, Wang X, Wu Y, Zhou X, Fu W, Liu L, Hu HG, Chen YG. 	A PROTAC peptide induces durable β-catenin degradation and suppresses Wnt-dependent intestinal cancer	Stapled AMP						
DRAMP35727	RRWPRⓍILDⓍHVRRVWR	RRWPRXILDXHVRRVWR	XRRWPRSILDSHVRRVWR	17	xStAx, aStAx-35R	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(6) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	32550000	Cell Discov. 2020 Jun 9;6:37.	Liao H, Li X, Zhao L, Wang Y, Wang X, Wu Y, Zhou X, Fu W, Liu L, Hu HG, Chen YG. 	A PROTAC peptide induces durable β-catenin degradation and suppresses Wnt-dependent intestinal cancer	Stapled AMP						
DRAMP35728	RRWPRⓍlLDⓍHVRRVWRXALAPYIP	RRWPRXlLDXHVRRVWRXALAPYIP	RRWPRSlLDSHVRRVWRXALAPYIP	25	xStAx-VHLL	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Inhibit wnt/β-catenin signaling pathway		Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(6) and Ⓧ (10) are cross-linked by hydrocarbon stapling	Mix	Not available	32550000	Cell Discov. 2020 Jun 9;6:38.	Liao H, Li X, Zhao L, Wang Y, Wang X, Wu Y, Zhou X, Fu W, Liu L, Hu HG, Chen YG. 	A PROTAC peptide induces durable β-catenin degradation and suppresses Wnt-dependent intestinal cancer	Stapled AMP						
DRAMP35749	GⓍFAVIKKⓍASVIKGL	GXFAVIKKXASVIKGL	GRFAVIKKSASVIKGL	16	A4K14-citropin1.1-Sp6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=23.78 μM); A549 (IC50=30.19 μM); U87 (IC50=34.49 μM); C4-2B (IC50=35.84 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(2) and Ⓧ (9) are cross-linked by hydrocarbon stapling	L	Not available	33363118	 Front Chem. 2020 Dec 10;8:616147.	Wang N, Xie G, Liu C, Cong W, He S, Li Y, Fan L, Hu HG. 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						
DRAMP35750	GLFAVⓍKKVASVⓍKGL	GLFAVXKKVASVXKGL	GLFAVRKKVASVSKGL	16	A4K14-citropin1.1-Sp7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=12.1 μM); U87 (IC50=14.72 μM); A549 (IC50=16.37 μM); C4-2B (IC50=35.84 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(6) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Not available	33363118	 Front Chem. 2020 Dec 10;8:616148.	Wang N, Xie G, Liu C, Cong W, He S, Li Y, Fan L, Hu HG. 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						
DRAMP35751	GLFAVⓍKKVASVⓍKGL	GLFAVXKKVASVXKGL	GLFAVRKKVASVSKGL	16	A4K14-citropin1.1-Sp7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 (IC50=7.44µM); MCF-7 (IC50=7.47µM); U-87MG ATCC (IC50=9.2µM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(6) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Not available	33363118	 Front Chem. 2020 Dec 10;8:616148.	Wang N, Xie G, Liu C, Cong W, He S, Li Y, Fan L, Hu HG. 	Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides	Stapled AMP						
DRAMP35824	ILGKLLⓍTAAⓍLLSNL	ILGKLLXTAAXLLSNL	/	16	Alyteserin-2a-Sp1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MDA-MB-231 (IC50=1.6μM); A549 (IC50=3.6±1.0 μM); MCF-7  (IC50=4.9±0.91 μM); U87 (IC50=9.8±0.11 μM)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ are cross-linked by hydrocarbon stapling	L	Not available	34989078	J Pept Sci. 2022 Jul;28(7):e3401	Yu Z, Tang H, Cong W, Gao F, Li H, Hu H, Wang X, He S.	Hydrocarbon stapling modification of peptide alyteserin-2a: Discovery of novel stapled peptide antitumor agents	Stapled AMP						
DRAMP35825	ILⓍKLLⓍTAAGLLSNL	ILXKLLXTAAGLLSNL	/	16	Alyteserin-2a-Sp2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: A549 (IC50=10.9±2.7 μM); MDA-MB-231 (IC50=3.6μM); U87 (IC50=5.2±0.68 μM); MCF-7  (IC50=5.8±0.80 μM)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ are cross-linked by hydrocarbon stapling	L	Not available	34989078	J Pept Sci. 2022 Jul;28(7):e3402	Yu Z, Tang H, Cong W, Gao F, Li H, Hu H, Wang X, He S.	Hydrocarbon stapling modification of peptide alyteserin-2a: Discovery of novel stapled peptide antitumor agents	Stapled AMP						
DRAMP35826	ILGKLLSTAⓍGLLⓍNL	ILGKLLSTAXGLLXNL	/	16	Alyteserin-2a-Sp3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MDA-MB-231 (IC50=0.86μM); MCF-7  (IC50=0.99±0.21 μM); A549 (IC50=2.8±0.90 μM); U87 (IC50=3.9±0.010 μM)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ are cross-linked by hydrocarbon stapling	L	Not available	34989078	J Pept Sci. 2022 Jul;28(7):e3403	Yu Z, Tang H, Cong W, Gao F, Li H, Hu H, Wang X, He S.	Hydrocarbon stapling modification of peptide alyteserin-2a: Discovery of novel stapled peptide antitumor agents	Stapled AMP						
DRAMP35827	ILGKLLⓍTAAGLLⓍNL	ILGKLLXTAAGLLXNL	/	16	Alyteserin-2a-Sp4	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: U87 (IC50=10.1±1.6 μM); A549 (IC50=11.6±2.2 μM); MCF-7  (IC50=8.5±1.4 μM); MDA-MB-231 (IC50=9.2μM)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(7) and Ⓧ (14) are cross-linked by hydrocarbon stapling	L	Not available	34989078	J Pept Sci. 2022 Jul;28(7):e3404	Yu Z, Tang H, Cong W, Gao F, Li H, Hu H, Wang X, He S.	Hydrocarbon stapling modification of peptide alyteserin-2a: Discovery of novel stapled peptide antitumor agents	Stapled AMP						
DRAMP35828	ILⓍKLLSTAⓍGLLSNL	ILXKLLSTAXGLLSNL	/	16	Alyteserin-2a-Sp5	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=5.2±0.91 μM); A549 (IC50=8.4±1.8 μM); U87 (IC50=9.5±2.0 μM)	Not available	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(3) and Ⓧ (10) are cross-linked by hydrocarbon stapling	L	Not available	34989078	J Pept Sci. 2022 Jul;28(7):e3405	Yu Z, Tang H, Cong W, Gao F, Li H, Hu H, Wang X, He S.	Hydrocarbon stapling modification of peptide alyteserin-2a: Discovery of novel stapled peptide antitumor agents	Stapled AMP						
DRAMP35849	VⓍRFKⓍFFRKLKKLV	VXRFKXFFRKLKKLV	VSRFKSFFRKLKKLV	15	B1-L-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: U87 (IC50=12.24±1.23 μM); Huh-7 (IC50=13.87±1.25 μM); MCF-7  (IC50=15.89±0.92 μM)	HC50>80 μM	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ are cross-linked by hydrocarbon stapling	L	Not available	35464194	 Erratum in: Front Chem. 2023 Oct 27;11:1285116. 	Su Z, Liu C, Cong W, He S, Su L, Hu H.	Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides	Stapled AMP						
DRAMP35850	VKRFⓍKFFⓍKLKKLV	VKRFXKFFXKLKKLV	VKRFSKFFSKLKKLV	15	B1-L-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: Huh-7 (IC50=6.18±0.63 μM); MCF-7  (IC50=6.591±0.42 μM); U87 (IC50=8.86±1.43 μM)	HC50>80 μM	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ are cross-linked by hydrocarbon stapling	L	Not available	35464194	 Erratum in: Front Chem. 2023 Oct 27;11:1285117. 	Su Z, Liu C, Cong W, He S, Su L, Hu H.	Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides	Stapled AMP						
DRAMP35851	VKRFKⓍFFRⓍLKKLV	VKRFKXFFRXLKKLV	VKRFKSFFRSLKKLV	15	B1-L-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: U87 (IC50=3.59±1.20 μM); MCF-7  (IC50=5.478±0.89 μM); Huh-7 (IC50=5.96±0.54 μM)	HC50>80 μM	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ are cross-linked by hydrocarbon stapling	L	Not available	35464194	 Erratum in: Front Chem. 2023 Oct 27;11:1285118. 	Su Z, Liu C, Cong W, He S, Su L, Hu H.	Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides	Stapled AMP						
DRAMP35852	VKRFKKFFⓍKLKⓍLV	VKRFKKFFXKLKXLV	VKRFKKFFSKLKSLV	15	B1-L-4	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: Huh-7 (IC50=13.41±1.92 μM); MCF-7  (IC50=15.20±1.02 μM); U87 (IC50=17.91±3.23 μM)	HC50>80 μM	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ are cross-linked by hydrocarbon stapling	L	Not available	35464194	 Erratum in: Front Chem. 2023 Oct 27;11:1285119. 	Su Z, Liu C, Cong W, He S, Su L, Hu H.	Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides	Stapled AMP						
DRAMP35853	VⓍRFKKFFⓍKLKKLV	VXRFKKFFXKLKKLV	VRRFKKFFSKLKKLV	15	B1-L-5	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: Huh-7 (IC50=13.84±1.53 μM); MCF-7  (IC50=13.99±0.73 μM); U87 (IC50=14.33±2.35 μM)	HC50>80 μM	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(2) and Ⓧ (9) are cross-linked by hydrocarbon stapling	L	Not available	35464194	 Erratum in: Front Chem. 2023 Oct 27;11:1285120. 	Su Z, Liu C, Cong W, He S, Su L, Hu H.	Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides	Stapled AMP						
DRAMP35854	VKRFⓍKFFRKLⓍKLV	VKRFXKFFRKLXKLV	VKRFRKFFRKLSKLV	15	B1-L-6	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: U87 (IC50=4.58±0.93 μM); MCF-7  (IC50=5.152±1.04 μM); Huh-7 (IC50=5.89±0.43 μM)	HC50>80 μM	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(5) and Ⓧ (12) are cross-linked by hydrocarbon stapling	L	Not available	35464194	 Erratum in: Front Chem. 2023 Oct 27;11:1285121. 	Su Z, Liu C, Cong W, He S, Su L, Hu H.	Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides	Stapled AMP						
DRAMP35855	VKRFKⓍFFRKLKⓍLV	VKRFKXFFRKLKXLV	VKRFKRFFRKLKSLV	15	B1-L-7	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: U87 (IC50=12.70±1.63 μM); MCF-7  (IC50=13.36±1.22 μM); Huh-7 (IC50=7.49±1.2 μM)	HC50>80 μM	Cyclic (Stapled)	Free	Amidation	Stapled: Ⓧ(6) and Ⓧ (13) are cross-linked by hydrocarbon stapling	L	Not available	35464194	 Erratum in: Front Chem. 2023 Oct 27;11:1285122. 	Su Z, Liu C, Cong W, He S, Su L, Hu H.	Design, Synthesis, and Antitumor Activity Study of All-Hydrocarbon-Stapled B1-Leu Peptides	Stapled AMP						
DRAMP35884	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=82.1 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6684.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35885	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=85.1 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6684.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35886	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=57.7 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6684.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35887	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=82.1 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6685.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35888	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=85.1 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6685.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35889	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=57.7 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6685.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35890	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=82.1 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6686.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35891	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=85.1 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6686.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35892	TSFⓍEYWⓍLLSXLAXYXP	TSFXEYWXLLSXLAXYXP	TSFSEYWSLLSXLAXYXP	18	SPMI-HIF1-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=57.7 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6686.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35893	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=6.7 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6687.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35894	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=10.8 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6687.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35895	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=15.2 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6687.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35896	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=6.7 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6688.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35897	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=10.8 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6688.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35898	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=15.2 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6688.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35899	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=6.7 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6689.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35900	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=10.8 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6689.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35901	TSFⓍEYWALLⓍXLAXYXP	TSFXEYWALLXXLAXYXP	TSFREYWALLSXLAXYXP	18	SPMI-HIF2-3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=15.2 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6689.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35902	TSFⓍEYWⓍLLS	TSFXEYWXLLS	TSFSEYWSLLS	11	SPMI1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53-/- (IC50>100 μM); HCT 116 p53+/+ (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6690.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35903	TSFⓍEYWALLⓍ	TSFXEYWALLX	TSFREYWALLS	11	SPMI2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: HCT 116 p53+/+ (IC50=28.4 μM); HCT 116 p53-/- (IC50>100 μM)	Not available	Cyclic (Stapled)	Acetylation	Amidation	Stapled: Ⓧ(4) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36185610	Theranostics. 2022 Sep 11;12(15):6665-6691.	Chen S, Li X, Li Y, Yuan X, Geng C, Gao S, Li J, Ma B, Wang Z, Lu W, Hu HG.	Design of stapled peptide-based PROTACs for MDM2/MDMX atypical degradation and tumor suppression	Stapled AMP						
DRAMP35912	TEⓍQTNⓍVP	TEXQTNXVP	TESQTNSVP	9	SHP1	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(3) and Ⓧ (7) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13883. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35913	FRRKAFⓍHWYⓍG	FRRKAFXHWYXG	FRRKAFSHWYSG	12	SHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=37.21 ± 2.66 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13884. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35914	VPKⓍVNAⓍIA	VPKXVNAXIA	VPKSVNASIA	10	SHP3	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13885. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35915	VPⓍLTQⓍMF	VPXLTQXMF	VPSLTQSMF	9	SHP4	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(3) and Ⓧ (7) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13886. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35916	NEAⓍYDIⓍFR	NEAXYDIXFR	NEASYDISFR	10	SHP5	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Not available	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(4) and Ⓧ (8) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13887. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35917	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	FSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=3.71 ± 0.21 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13888. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35918	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	FSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=18.69 ± 1.27 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13888. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35919	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	FSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=33.79 ± 2.34 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13888. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35920	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	FSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=52.33 ± 3.75 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13888. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35921	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ClSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=3.71 ± 0.21 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13889. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35922	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ClSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=18.69 ± 1.27 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13889. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35923	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ClSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=33.79 ± 2.34 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13889. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35924	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ClSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=52.33 ± 3.75 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13889. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35925	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	BrSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=3.71 ± 0.21 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13890. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35926	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	BrSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=18.69 ± 1.27 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13890. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35927	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	BrSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=33.79 ± 2.34 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13890. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35928	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	BrSHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=52.33 ± 3.75 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13890. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35929	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ISHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=3.71 ± 0.21 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13891. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35930	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ISHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=18.69 ± 1.27 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13891. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35931	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ISHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=33.79 ± 2.34 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13891. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP						
DRAMP35932	XRRKAFⓍHWYⓍG	XRRKAFXHWYXG	XRRKAFSHWYSG	12	ISHP2	Not available		Synthetic construct	Antimicrobial, Anticancer		No specific results about the strcture presented in the forms of tables, graphs or words	No other descriptive information about the structure found in the literature	Not available	Not available	Tumor cells: MCF-7  (IC50=52.33 ± 3.75 μM)	Not available	Cyclic (Stapled)	FITC, 5(6)-carboxy fluorescence	Free	Stapled: Ⓧ(7) and Ⓧ (11) are cross-linked by hydrocarbon stapling	L	Not available	36240440	J Med Chem. 2022 Oct 27;65(20):13866-13891. 	Adak A, Das G, Gupta V, Khan J, Mukherjee N, Mondal P, Roy R, Barman S, Gharai PK, Ghosh S. 	Evolution of Potential Antimitotic Stapled Peptides from Multiple Helical Peptide Stretches of the Tubulin Heterodimer Interface: Helix-Mimicking Stapled Peptide Tubulin Inhibitors	Stapled AMP