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. 2002 Nov;46(11):3585-90.
doi: 10.1128/AAC.46.11.3585-3590.2002.

Cationic hydrophobic peptides with antimicrobial activity

Margareta Stark  1 , Li-Ping Liu, Charles M Deber
Affiliations

Cationic hydrophobic peptides with antimicrobial activity

Margareta Stark et al. Antimicrob Agents Chemother. 2002 Nov.

Abstract

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

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Figures

FIG. 1.
FIG. 1.
CD spectra of the F17-6K peptide in an aqueous buffer (Aq) containing 20 mM Tris-HCl and 20 mM NaCl, pH 7.4, and in the same buffer with the addition of 20 mM SDS. The spectrum of all-d F17-6K in SDS is presented for comparison. [θ], ellipticity (measured in degrees × square centimeter per decimole). The peptide concentration was 30 to 40 μM, with an estimated uncertainty of ±5%. Spectra are as indicated on the diagram. See the text for a further discussion.
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