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Original Sequence
- VNWKKILGKIIKVVK
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Source
- Synthetic construct
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Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
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- Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.
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Target Organism
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- [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).
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Hemolytic Activity
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- [Ref.22526241] LC50 = 31.3 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.
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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: 6 and 10) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling.
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Secondary Structure
- ①20% α-helical content in water. ②55% α-helical content in 50% TFE. ③55% α-helical content in 8mM SDS.
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Structure Description
- 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.
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There is no predicted structure for DRAMP21486.
- Literature 1
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Title
- Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera
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Reference
- Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 18.
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Author
- Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský