General Information
-
DRAMP ID
- DRAMP21352
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Peptide Name
- 3IH2 (De Novo Synthesis)
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Source
- synthetic construct
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Family
- Not found
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Gene
- Not found
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Sequence
- IHHIHHIIHHIHHI
-
Sequence Length
- 14
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UniProt Entry
- No entry found
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Protein Existence
- Synthetic form
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram-
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Target Organism
-
- [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC=4μM), Escherichia coli UB1005 (MIC=8μM), Escherichia coli K88 (MIC=4μM), Escherichia coli K99 (MIC=4μM), Escherichia coli 078 (MIC=8μM), Escherichia coli 987P (MIC=2μM), Pseudomonas aeruginosa 27853 (MIC=4μM), Pseudomonas aeruginosa PAO1 (MIC=4μM), Salmonella typhimurium 14028 (MIC=32μM), Salmonella typhimurium 7731 (MIC=16μM)
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Hemolytic Activity
-
- [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells
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Cytotoxicity
-
- [Ref.31199117] ①The cell viability of HEK293T cells induced by 3IH2 is 105.8%, 105.8%, 105.2%, 104.2%, 101.1%, 101.7% and 100.8% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 3IH2 is 106.2%, 105.9%, 105.9%, 105.6%, 104.2%, 104.8% and 101.4% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM.
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Linear
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N-terminal Modification
- Free
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C-terminal Modification
- Amidation
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Nonterminal Modifications and Unusual Amino Acids
- None
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Stereochemistry
- L
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Structure
- 95% α-helix in 50% TFE/H2O
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Structure Description
- The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”.
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP21352.
Physicochemical Information
-
Formula
- C84H124N30O15
Absent Amino Acids
- ACDEFGKLMNPQRSTVW
Common Amino Acids
- H
Mass
- 1794.1
PI
- 7.28
Basic Residues
- 8
Acidic Residues
- 0
Hydrophobic Residues
- 6
Net Charge
- +8
-
Boman Index
- -776
Hydrophobicity
- 0.1
Aliphatic Index
- 167.14
Half Life
-
- Mammalian:20 hour
- Yeast:30 min
- E.coli:>10 hour
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 0
DRAMP21352
Comments Information
Function
- Antibacterial activity against Gram-negative bacteria.
Literature Information
- ·Literature 1
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Title
- Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition
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Pubmed ID
- 31199117
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Reference
- ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14.
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Author
- Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L.