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MYP_007323
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Basic Information
MEP-Ns-5
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antifungal
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Venom / Toxin ▸ General toxin ▸ Toxic
Standard
18 amino acids
C93H162N24O20S2
Standard
Sequence
GFLSILKKVLGKVMAHMK
Physicochemical Analysis
2000.56 Da
10.48
3.84
3.58
0.2135
0.68
0.54
0.23
3.42
124.44
0.0556
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
711.01
-2.36
25.0
27.0
72.0
139.0
2.0
17.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0010882 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
MEP
32630
Structure & Mods
hydrocarbon-stapled side-chain cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Amidation
The J (position: 14) in sequence indicates norleucine. Ⓧ (position: 5, 9, 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively
Bio-Activity Profile
Hemolytic
human red blood cells
29 μM
LC50
PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 33. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0078829 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
MEP
32630
Structure & Mods
hydrocarbon-stapled side-chain cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Amidation
The J (position: 14) in sequence indicates norleucine. Ⓧ (position: 5, 9, 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively
Bio-Activity Profile
Antimicrobial Antibacterial
Pseudomonas aeruginosa
>100 μM
MIC
PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 33. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0083987 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
MEP
32630
Structure & Mods
hydrocarbon-stapled side-chain cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Amidation
The J (position: 14) in sequence indicates norleucine. Ⓧ (position: 5, 9, 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively
Bio-Activity Profile
Antimicrobial Antibacterial
Bacillus subtilis
1.2 μM
MIC
PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 33. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0145437 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
MEP
32630
Structure & Mods
hydrocarbon-stapled side-chain cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Amidation
The J (position: 14) in sequence indicates norleucine. Ⓧ (position: 5, 9, 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively
Bio-Activity Profile
Antimicrobial Antibacterial
Escherichia coli
5.6 μM
MIC
PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 33. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0163738 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
MEP
32630
Structure & Mods
hydrocarbon-stapled side-chain cyclic peptide [Cyclic]
canonical L-amino-acid peptide [L]
None
Amidation
The J (position: 14) in sequence indicates norleucine. Ⓧ (position: 5, 9, 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively
Bio-Activity Profile
Antimicrobial Antibacterial
Staphylococcus aureus
57 μM
MIC
PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 33. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
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