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MYP_051707
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Basic Information
D-LAK120
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
C140H254N34O26
Standard
Sequence
KKLALLALKKWLLALKKLALLALKK
Physicochemical Analysis
2829.73 Da
10.85
7.75
7.54
0.3101
0.75
0.58
0.14
-2.44
191.60
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
985.67
1.40
35.0
34.0
105.0
200.0
2.0
24.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0013448 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 Antiparasitic Antiprotozoal Anti-Gram-negative
Escherichia coli NCTC 9001
1.48 ± 0.53 μM
MIC50
PMID22869378 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22869378/
RECORD: Rec_0019663 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 Antiparasitic Antiprotozoal Anti-Gram-negative
Pseudomonas aeruginosa PAO1
2.71 ± 1.07 μM
MIC50
PMID22869378 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22869378/
RECORD: Rec_0038054 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 Hemolytic
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_0042706 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
3.3 μM
EC50
PMID25154927 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/25154927/
RECORD: Rec_0050665 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
D-LAK120
32630
Structure & Mods
linear peptide [Linear]
all-D amino-acid peptide [D]
None
Amidation
Bio-Activity Profile
Antimicrobial Antiparasitic Antimalarial
Plasmodium falciparum 3D7
1.95±0.08 μM
IC50; Fluorimetry (SYBR Green II)
PaperConformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic alpha-helical peptides PMID22869378 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22869378/
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