Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 17, Issue 3, Pages 211-217Publisher
WILEY-BLACKWELL
DOI: 10.1002/psc.1314
Keywords
antimicrobial peptide; gramicidin S; amphipathicity; cyclic peptide synthesis; NMR; molecular dynamics; hemolysis; structure-activity relationship
Funding
- Ministry of Science and Academic Education of Poland [BW/8000-5-0111-8]
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Gramicidin S (GS) is a cyclo-decapeptide antibiotic isolated from Bacillus brevis. The structural studies have shown that GS forms a two-stranded antiparallel beta-sheet imposed by two II' beta-turns. Despite its wide Gram+ and Gram- antimicrobial spectrum, GS is useless in therapy because of its high hemotoxicity in humans. It was found, however, that the analogues of GS-14 (GS with 14 amino acid residues) attained a better antimicrobial selectivity when their amphipatic moments were perturbed. In this study, we report effects of similar perturbations imposed on GS cyclo-decapeptide analogues. Having solved their structures by NMR/molecular dynamics and having tested their activities/selectivities, we have concluded that the idea of perturbation of the amphipatic moment does not work for GS-10_0 analogues. An innovative approach to the synthesis of head-to-tail cyclopeptides was used. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.
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