General Information
-
DRAMP ID
- DRAMP21495
-
Peptide Name
- MEP-Ns-1
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Sequence
- GFLSILKKVLPKⓍJAHⓍK
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Sequence Length
- 18
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Original Sequence
- GFLSILKKVLPKVMAHMK
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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 = 0.8 μM), Bacillus subtilis (MIC = 1.1 μM), Staphylococcus aureus (MIC = 10.8 μM);
- Gram-negative bacteria: E.coli (MIC = 2.5 μM), Pseudomonas aeruginosa (MIC = 77 μM);
- Fungi: Candida albicans (MIC = 30 μM).
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Hemolytic Activity
-
- [Ref.22526241] LC50 = 18.1 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 J (position: 14) in sequence indicates norleucine. ②The Ⓧ (position: 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling.
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Stereochemistry
- L
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Secondary Structure
- ①19% α-helical content in water.②66% α-helical content in 50% TFE. ③75% α-helical content in 8mM SDS.
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Structure Description
- The CD spectra of the singly stapled peptides of the i, i + 4 type acquired in water show a slight increase (by 5 %) of helical content in the case of MEP-Ns-1, MEP-Ns-2 and LL-IIIs-3 compared to their unstapled precursors.
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Helical Wheel Diagram
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Predicted Structure
- Please click DRAMP21495 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
- C₁₀₁H₁₇₂N₂₄O₂₀
Absent Amino Acids
- CDEMNQRTWY
Common Amino Acids
- K
Mass
- 2040.33
PI
- /
-
Basic Residues
- 5
Acidic Residues
- 0
Hydrophobic Residues
- 7
Hydrophobicity
- /
Polar Residues
- 2
DRAMP21495
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 28.
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Author
- Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský