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MYP_163869
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Basic Information
D-LAK120-H
Anticancer
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Mycobacterium
Antiparasitic ▸ Antimalarial
Antiparasitic ▸ Antiprotozoal
Antiparasitic ▸ Antiprotozoal ▸ Antimalarial ▸ Anti-Plasmodium
Antiparasitic ▸ General antiparasitic ▸ Antiparasitic
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Standard
25 amino acids
C140H242N40O26
Standard
Sequence
KKLALHALKKWLHALKKLAHLALKK
Physicochemical Analysis
2901.67 Da
10.85
8.01
7.65
0.3205
-0.09
0.72
-0.03
-5.84
144.80
0.0400
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
1071.71
-1.84
38.0
37.0
105.0
206.0
5.0
24.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0324411 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Synthetic designed peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antimycobacterial
Mycobacterium tuberculosis XDR strain WYC-11
25 μM
IC50
PMID25154927 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25154927/
RECORD: Rec_0332870 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Synthetic designed peptide
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antimycobacterial
Mycobacterium tuberculosis XDR strain
5.5 μM
EC50
PMID25154927 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25154927/
RECORD: Rec_0393752 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-negative Antiplasmodial
Pseudomonas aeruginosa
1.35±0.07 μM
MIC
PaperConformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic alpha-helical peptides. J Biol Chem. 2012 Oct 5;287(41):34120-34133. doi: 10.1074/jbc.M112.359067. PMID: 22869378. PMID22869378 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22869378/
RECORD: Rec_0406545 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-negative Antiplasmodial
Escherichia coli NCTC 9001
1.54±0.01 μM
MIC
PaperConformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic alpha-helical peptides. J Biol Chem. 2012 Oct 5;287(41):34120-34133. doi: 10.1074/jbc.M112.359067. PMID: 22869378. PMID22869378 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22869378/
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