Peptide Database

Peptide NameD-LAK60

Function Ontology

Antimicrobial

Antimicrobial ▸ Antibacterial

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative

Standard StatusStandard

Sequence Length25 amino acids

Chemical FormulaC140H254N34O26

DescriptionStandard

        KKLALKALLLWLKALLKLAKLALKK
    

Molecular Weight2829.73 Da

Isoelectric Point (pI)10.85

Net Charge (pH 7.0)7.75

Net Charge (pH 7.4) 7.54

Charge Density (pH 7.0) 0.3101

GRAVY Index0.75

Hydrophobic Moment 0.60

Boman Index0.14

Instability Index0.24

Aliphatic Index 191.60

Aromaticity 0.0400

Extinction Coeff. Reduced 5500.00

Extinction Coeff. Oxidized 5500.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

TPSA 985.67

LogP 1.40

H-bond Donors 35.0

H-bond Acceptors 34.0

Rotatable Bonds 105.0

Heavy Atoms 200.0

Ring Count 2.0

Amide Bonds 24.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0021512 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configtopology not specified [Not included yet]

Chiralitystereochemistry not specified [Other]

Bio-Activity Profile

Function

Antimicrobial Antibacterial Anti-Gram-negative

TargetPseudomonas aeruginosa

Activity22.62 μM

MethodMIC

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_0086992 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configtopology not specified [Not included yet]

Chiralitystereochemistry not specified [Other]

Bio-Activity Profile

Function

Antimicrobial Antibacterial Anti-Gram-negative

TargetEscherichia coli NCTC 9001

Activity22.62 μM

MethodMIC

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_0279568 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configtopology not specified [Not included yet]

Chiralitystereochemistry not specified [Other]

Bio-Activity Profile

Function

Antimicrobial Antibacterial Anti-Gram-negative

TargetEscherichia coli Top 10

MethodMIC

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/