Cramp Analog Having Potent Antibiotic Activity without Hemolytic Activity

Title: Cramp Analog Having Potent Antibiotic Activity without Hemolytic Activity

Volume: 9 Issue: 4

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

Affiliation:

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

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.

Cite this article as:

Kang Shin-Won, Lee Gun Dong, Yang Sung-Tae, Kim Yangmee, Kim Il. Jae, Hahm Kyung-Soo and Shin Yub Song, Cramp Analog Having Potent Antibiotic Activity without Hemolytic Activity, Protein & Peptide Letters 2002; 9 (4) . https://dx.doi.org/10.2174/0929866023408643