Aug 24, 2012

Effect of repetitive lysine-tryptophan motifs on the bactericidal activity of antimicrobial peptides

Amino Acids
Ramamourthy GopalYoonkyung Park

Abstract

Previous studies identified lysine- and tryptophan-rich sequences within various cationic antimicrobial peptides. In the present study, we synthesized a series of peptides composed of lysine (K)-tryptophan (W) repeats (KW)( n ) (where n equals 2, 3, 4 or 5) with amidation of the C-terminal to increase cationicity. We found that increases in chain length up to (KW)(4) enhanced the peptides' antibacterial activity; (KW)(5) exhibited somewhat less bactericidal activity than (KW)(4). Cytotoxicity, measured as lysis of human red blood cells, also increased with increasing chain length. With (KW)(5), reduced antibacterial activity and increased cytotoxicity correlated with greater hydrophobicity and self-aggregation in the aqueous environment. The peptides acted by inducing rapid collapse of the bacterial transmembrane potential and induction of membrane permeability. The mode of interaction of the peptides and the phosphate groups of lipopolysaccharide was dependent upon the peptides' ability to permeate the membrane. Longer peptides [(KW)(4) and (KW)(5)] but not shorter peptides [(KW)(2) and (KW)(3)] strongly bound and partially inserted into negatively charged, anionic lipid bilayers. These longer peptides also induced membrane pe...Continue Reading

Mentioned in this Paper

Pathologic Cytolysis
Tryptophan
Tissue Membrane
Carboxy-Terminal Amino Acid
Aggregation
Red blood cells, blood product
Phosphate Measurement
Lysine
Bactericidal Activity
Vesicle

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