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MYP_035420
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Basic Information
L-K6 L5L11W
Antimicrobial
Antimicrobial ▸ Antibacterial
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Standard
13 amino acids
C85H143N21O15
Standard
Sequence
IKKIWSKIKKWLK
Physicochemical Analysis
1699.18 Da
10.70
5.75
5.54
0.4426
-0.67
0.78
-0.18
-13.93
120.00
0.1538
11000.00
11000.00
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
620.45
0.61
23.0
21.0
62.0
121.0
4.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0214199 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
Staphylococcus epidermidis
2.50 μM
MIC
PaperInvestigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action.
RECORD: Rec_0215727 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
Escherichia coli
2.50 μM
MIC
PaperInvestigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action.
RECORD: Rec_0223943 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
E.cloacae
>100 μM
MIC
PaperInvestigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action.
RECORD: Rec_0247337 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
Klebsiella pneumoniae
>100 μM
MIC
PaperInvestigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action.
RECORD: Rec_0264779 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
B. cereus
18.75 μM
MIC
PaperInvestigation of the role of tryptophan residues in cationic antimicrobial peptides to determine the mechanism of antimicrobial action.
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