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MYP_173781
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Basic Information
Unnamed
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Venom / Toxin ▸ General toxin ▸ Toxic
not Standard
18 amino acids
-
contains X representing unresolved or non-standard residue
Sequence
GFLSILKKVLPKVXAHXK
Physicochemical Analysis
0.00 Da
0.00
0.00
0.00
0.00
0.00
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Residue Composition
Amino Acid Composition
Chemical Descriptors
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0335172 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Nle= norleucine, Met (O)= methionine sulfoxide
Bio-Activity Profile
Antimicrobial
Rat erythrocytes
200 μM
LC50
Paperhttps://pubmed.ncbi.nlm.nih.gov/20499256/ PMID20499256 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20499256/
RECORD: Rec_0361020 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
The J (position: 14 and 17) in sequence are norleucine
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal
Gram-positive bacteria: Micrococcus luteus
1 μM
MIC
PaperEffect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0375635 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct [Synthetic]
32630
Structure & Mods
topology not specified [Not included yet]
stereochemistry not specified [Other]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal
PaperEffect 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. doi: 10.1007/s00726-012-1283-1. PMID: 22526241. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0380401 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct [Synthetic]
32630
Structure & Mods
topology not specified [Not included yet]
stereochemistry not specified [Other]
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal
Escherichia coli
0.9 μM
MIC
PaperEffect 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. doi: 10.1007/s00726-012-1283-1. PMID: 22526241. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0380425 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
The J (position: 14 and 17) in sequence are norleucine
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal
Escherichia coli
0.9 μM
MIC
PaperEffect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
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