‹ ›
MYP_102243
← PREVIOUS NEXT → BACK
Basic Information
LL-IIIs-6a
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
C73H135N21O21
Standard
Sequence
VNSKKISPKSIKVSK
Physicochemical Analysis
1642.98 Da
10.60
4.73
4.51
0.3153
-0.69
0.45
-0.26
21.65
90.67
0.0000
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
716.04
-8.41
25.0
26.0
60.0
115.0
1.0
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_0090611 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
0.8 μM
MIC
PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0102432 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Hemolytic
Hemolytic activity
82 μM
LC50
PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/
RECORD: Rec_0106402 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 Hemolytic
human red blood cells
82 μM
LC50
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_0116551 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
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_0118444 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 Hemolytic
human red blood cells
100 μM
LC50
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/
FIRST PREV 1 2 3 4 ... 6 NEXT LAST
Showing 5 records on this page · Page 2 of 6