‹ ›
MYP_139023
← PREVIOUS NEXT → BACK
Basic Information
LL-IIIs-2 (lasioglossin III peptide derivative)
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
Standard
15 amino acids
C81H142N22O19
Standard
Sequence
VNWKKILGKSIKVSK
Physicochemical Analysis
1728.13 Da
10.60
4.73
4.51
0.3153
-0.31
0.59
-0.09
-7.38
116.67
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
700.16
-4.50
25.0
24.0
63.0
122.0
2.0
15.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0158457 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 Hemolytic
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_0158837 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
Micrococcus luteus
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_0242639 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Bacillus cereus
1.2 μM
MIC
PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0253580 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Pseudomonas aeruginosa
86.7 μM
MIC
PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0274277 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Escherichia coli
8.8 μM
MIC
PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
FIRST PREV 1 2 3 4 NEXT LAST
Showing 5 records on this page · Page 2 of 4