Cationic Hydrophobic Peptides with Antimicrobial Activity

Cationic polymerization Anti-Infective Agents
DOI: 10.1128/aac.46.11.3585-3590.2002 Publication Date: 2002-10-16T23:01:16Z
ABSTRACT
The MICs of cationic, hydrophobic peptides the prototypic sequence KKAAAXAAAAAXAAWAAXAAAKKKK-amide (where X is one 20 commonly occurring amino acids) are in a low micromolar range for panel gram-negative and gram-positive bacteria, with no or hemolytic activity against human rabbit erythrocytes. active only when average segmental hydrophobicity 19-residue core above an experimentally determined threshold value Phe, Trp, Leu, Ile, Met, Val, Cys, Ala). Antimicrobial could be increased by using that were truncated from prototype length to 11 residues, being Phe 6 Lys residues grouped at N terminus. We propose mechanism interaction between these bacterial membranes similar "carpet model," wherein interact anionic phospholipid head groups membrane surface portion peptide then able lipid bilayer, causing disruption membrane.
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