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Peptide Name
- MEP-Ns-4 trans
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Sequence
- GFⓏSILKKVⓍPKVJAHJK
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Original Sequence
- GFLSILKKVLPKVMAHMK
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Source
- Synthetic construct
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Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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- 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
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- [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 2 μM), Bacillus subtilis (MIC = 1.7 μM), Staphylococcus aureus (MIC = 63 μM);
- Gram-negative bacteria: E.coli (MIC = 16.3 μM), Pseudomonas aeruginosa (MIC ≥ 100 μM);
- Fungi: Candida albicans (MIC ≥ 100 μM).
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Hemolytic Activity
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- [Ref.22526241] LC50 = 20 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 J (position: 14 and 17) in sequence indicates norleucine. ②Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. ③Ⓩ (position: 3) is 2-(7'-pctenyl) lalnine in the R configuration. ④Ⓧ (10) and Ⓩ (3) are cross-linked by hydrocarbon stapling.
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Secondary Structure
- Unknown
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Structure Description
- No other descriptive information about the structure found in the literature
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- 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 32.
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Author
- Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský