General Information
-
DRAMP ID
- DRAMP21486
-
Peptide Name
- LL-IIIs-1
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Sequence
- VNWKKⓍLGKⓍIKVVK
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Sequence Length
- 15
-
Original Sequence
- VNWKKILGKIIKVVK
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Source
- Synthetic construct
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
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Comments
- Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.
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Target Organism
-
- [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
-
- [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
- No cytotoxicity information found in the reference(s) presented
Structure Information
-
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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Stereochemistry
- L
-
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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Helical Wheel Diagram
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Predicted Structure
- Please click DRAMP21486 predicted structure to download. The green ribbons represent the stapling amino acids, and the green bonds are the bridge linking two residues of stapling amino acids.
Physicochemical Information
-
Formula
- C₈₈H₁₅₂N₂₂O₁₇
Absent Amino Acids
- ACDEFHMPQRSTY
Common Amino Acids
- K
Mass
- 1790.32
PI
- /
-
Basic Residues
- 5
Acidic Residues
- 0
Hydrophobic Residues
- 6
Hydrophobicity
- /
Polar Residues
- 2
DRAMP21486
Literature Information
- 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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Pubmed ID
- 22526241
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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