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MYP_015185
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Basic Information
LL-IIIs-6b
Anticancer
Anticancer ▸ Cytotoxic anticancer activity ▸ Cytotoxic
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Toxicity / Safety ▸ Cytotoxicity ▸ Cytotoxic
Venom / Toxin ▸ General toxin ▸ Cytotoxic
Standard
15 amino acids
C89H156N22O17
Standard
Sequence
VNWKKILPKIIKVVK
Physicochemical Analysis
1806.33 Da
10.60
4.73
4.51
0.3153
0.29
0.78
0.07
3.54
162.00
0.0667
5500.00
5500.00
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
650.91
0.09
22.0
22.0
63.0
128.0
3.0
15.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0317617 VERIFIED: YES
Provenance & Taxonomy
Lasioglossum laticeps [Animal]
Lasioglossin III
88510.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Anticancer Antimicrobial Antifungal
SW colon cells
PaperToxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells | https://pubmed.ncbi.nlm.nih.gov/22100226/ PMID22100226 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22100226/
RECORD: Rec_0329904 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
LL-III
32630
Structure & Mods
hydrocarbon-stapled side-chain cyclic peptide [Cyclic]
cis S5-Pro8 conformationally modified peptide [Modified]
None
Amidation
The Ⓧ (position: 3, 7, 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (3) and Ⓧ (7), Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling respectively
Bio-Activity Profile
Hemolytic
human red blood cells
>100 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 24. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0347811 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 Anti-Gram-positive Anti-Gram-negative
Pseudomonas aeruginosa
100 μM
MIC
PMID19591185 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/19591185/
RECORD: Rec_0365480 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Lasioglossin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
Bio-Activity Profile
Anticancer Cytotoxic
CCRF-CEM
6±3 μM
IC50
PaperToxicity study of antimicrobial peptides from wild bee venom and their analogs toward mammalian normal and cancer cells PMID22100226 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22100226/
RECORD: Rec_0392195 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
LL-III
32630
Structure & Mods
hydrocarbon-stapled side-chain cyclic peptide [Cyclic]
cis S5-Pro8 conformationally modified peptide [Modified]
None
Amidation
The Ⓧ (position: 3, 7, 10 and 14) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (3) and Ⓧ (7), Ⓧ (10) and Ⓧ (14) are cross-linked by hydrocarbon stapling respectively
Bio-Activity Profile
Antimicrobial Antibacterial
Bacillus subtilis
1.1 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 24. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
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