General Information
-
DRAMP ID
- DRAMP28997
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Peptide Name
- Unstapled heptapeptide 1
-
Source
- Synthetic construct
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Family
- N/A
-
Gene
- N/A
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Sequence
- RWWWRWW
-
Sequence Length
- 7
-
UniProt Entry
- No entry found
-
Protein Existence
- Synthetic form
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+
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Target Organism
-
- Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 83 ± 18 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC > 100 μg/mL)
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
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Binding Target
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
-
Structure
- Helicity = 22.7% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM
-
Structure Description
- 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).
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP28997.
Physicochemical Information
-
Formula
- C67H76N18O8
Absent Amino Acids
- ACDEFGHIKLMNPQSTV
Common Amino Acids
- W
Mass
- 1261.46
PI
- 12
Basic Residues
- 2
Acidic Residues
- 0
Hydrophobic Residues
- 5
Net Charge
- +2
-
Boman Index
- -1819
Hydrophobicity
- -1.929
Aliphatic Index
- 0
Half Life
-
- Mammalian:1 hour
- Yeast:2 min
- E.coli:2 min
Extinction Coefficient Cystines
- 27500
Absorbance 280nm
- 4583.33
Polar Residues
- 0
DRAMP28997
Comments Information
Function
- Antibacterial activity against Gram-positive bacteria.
It is a heptapeptide designed rationally.
Literature Information
- ·Literature 1
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Title
- De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides
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Pubmed ID
- PubMed ID is not available
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Reference
- Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7.
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Author
- Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing