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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Cramp Analog Having Potent Antibiotic Activity without Hemolytic Activity

Author(s): Shin-Won Kang, Dong Gun Lee, Sung-Tae Yang, Yangmee Kim, Jae Il. Kim, Kyung-Soo Hahm and Song Yub Shin

Volume 9, Issue 4, 2002

Page: [275 - 282] Pages: 8

DOI: 10.2174/0929866023408643

Price: $65

Abstract

CRAMP-18 is an 18-residue functional region, corresponding to residues 16-33 of a mouse-derived antibiotic peptide CRAMP. To develop novel antibiotic peptides possessing strong antibiotic activity against bacterial, fungal and tumor cells without hemolytic activity, three analogs of CRAMP-18 were synthesized containing either Leu- or Lys-substitution. Leusubstitution ([L1, 8]-CRAMP-18) in the hydrophobic helix face of CRAMP-18 induced a dramatic increase in antibiotic activity without a significant increase in hemolytic activity. Lys-substitution ([K2, 13]-CRAMP-18 or [K9, 16]-CRAMP-18) in the hydrophilic helix face produced a smaller response. Therefore, [L1, 8]-CRAMP-18 may be an attractive candidate for developing novel peptide antibiotics.

Keywords: Cramp Analog, Hemolytic, peptide CRAMP, hydrophobic helix face

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