General Information
-
DRAMP ID
- DRAMP21489
-
Peptide Name
- LL-IIIs-4
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Sequence
- VNⓍKKIⓍGKⓍIKVⓍK
-
Sequence Length
- 15
-
Original Sequence
- VNWKKILGKIIKVVK
-
Source
- Synthetic construct
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
-
Comments
- Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.
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Target Organism
-
- [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 2 μM), Bacillus subtilis (MIC = 1.1 μM), Staphylococcus aureus (MIC = 80 μM);
- Gram-negative bacteria: E.coli (MIC = 20 μM), Pseudomonas aeruginosa (MIC > 100 μM);
- Fungi: Candida albicans (MIC > 100 μM).
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Hemolytic Activity
-
- [Ref.22526241] LC50 > 100 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: 3, 7, 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. ②Ⓧ (3) and Ⓧ (7), Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling respectively.
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Stereochemistry
- L
-
Secondary Structure
- ①45% α-helical content in water. ②48% α-helical content in 50% TFE. ③63% α-helical content in 8mM SDS.
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Structure Description
- On the other hand, the difference in α-helical content between doubly stapled analogs (LL-IIIs-4, MEP-Ns-3, MEP-Ns-5, and MEP-Ns-6) and their unstapled precursors is apparently higher, on average by 15 %
-
Helical Wheel Diagram
-
Predicted Structure
- There is no predicted structure for DRAMP21489.
Physicochemical Information
-
Formula
- C₈₆H₁₅₅N₂₁O₁₇
Absent Amino Acids
- ACDEFHLMPQRSTWY
Common Amino Acids
- K
Mass
- 1755.32
PI
- /
-
Basic Residues
- 5
Acidic Residues
- 0
Hydrophobic Residues
- 4
Hydrophobicity
- /
Polar Residues
- 2
DRAMP21489
Literature Information
- Literature 1
-
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 21.
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Author
- Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský