Journal
PEPTIDES
Volume 26, Issue 2, Pages 197-206Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2004.09.020
Keywords
antimicrobial peptide; homology modeling; structure-activity relationships
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The protegrin family of antimicrobial peptides is among the shortest in sequence length while remaining very active against a variety of microorganisms. The major goal of this study is to characterize easily calculated molecular properties, which quantitatively show high correlation with antibacterial activity. The peptides studied have high sequence similarity but vary in activity over more than an order of magnitude. Hence, sequence analysis alone cannot be used to predict activity for these peptides. We calculate structural properties of 62 protegrin and protegrin-analogue, peptides and correlate them to experimental activities against six microbe species. as well as hemolytic and cytotoxic activities. Natural protegnins structures were compared with synthetic derivatives using homology modeling, and property descriptors were calculated to determine the characteristics that confer their antimicrobial activity. A structure-activity relationship study of all these peptides provides information about the structural properties that affect activity against different microbial species. (C) 2004 Elsevier Inc. All rights reserved.
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