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Sequence
- KKKKKKAGFⓍAWAⓍFGA
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Original Sequence
- KKKKKKAAFAAWAAFAA
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Source
- Synthetic construct
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Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram-
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- Function: Antibacterial activity against Gram-negative bacteria. No experiments about antibacterial activity against Gram-positive bacteria are recorded.
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Target Organism
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- [Ref.29275987] Gram-negative bacteria: E. coli (MIC= 1.6 μM)
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Hemolytic Activity
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- [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.
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Cytotoxicity
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No cytotoxicity information found in the reference(s) presented
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Linear/Cyclic
- Cyclic (Stapled)
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N-terminal Modification
- Free
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C-terminal Modification
- Amidation
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Special Amino Acid and Stapling Position
- ①The Ⓧ (position: 10 and 14) in sequence indicates 2-(4'-pentenyl) alanine. ②Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling.
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Secondary Structure
- Lack of significant structure
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Structure Description
- 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
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There is no predicted structure for DRAMP21483.
- Literature 1
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Title
- Influence of hydrocarbon-stapling on membrane interactions of synthetic antimicrobial peptides
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Reference
- Bioorg Med Chem. 2018 Mar 15;26(6):1189-1196. doi: 10.1016/j.bmc.2017.10.020. Epub 2017 Oct 21.
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Author
- Tracy A Stone, Gregory B Cole, Huong Q Nguyen, Simon Sharpe, Charles M Deber