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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_0229143 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
Micrococcus luteus
1.5 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_0248256 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
Antifungal
Candida albicans
>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_0253188 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide; DSSP H 66.7%, E 0.0%, T 11.1%, C 22.2% [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Toxic Antimicrobial Hemolytic
PaperHemolytik: a database of experimentally determined hemolytic and non-hemolytic peptides PMID24174543 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/24174543/
RECORD: Rec_0318028 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Antimicrobial
Rat erythrocytes
41.4 μM
LC50
Paperhttps://pubmed.ncbi.nlm.nih.gov/18942691/ PMID18942691 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18942691/
RECORD: Rec_0371557 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
Bio-Activity Profile
Antimicrobial Antibacterial
PMID18942691 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18942691/
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