Journal
FEBS LETTERS
Volume 583, Issue 14, Pages 2425-2428Publisher
WILEY
DOI: 10.1016/j.febslet.2009.06.044
Keywords
Antimicrobial peptide; Cytolytic peptide; Hemolytic activity; Molecular modeling; Molecular hydrophobicity potential; Protein engineering
Funding
- Russian Foundation for Basic Research [07-0401166, 08-04-00454, 07-04-01514]
- Russian Federation Federal Agency for Science and Innovations [SS-4728.2006.4, MK-69.2008.4]
- RAS Programmes
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In silico structural analyses of sets of alpha-helical antimicrobial peptides (AMPs) are performed. Differences between hemolytic and non-hemolytic AMPs are revealed in organization of their N-terminal region. A parameter related to hydrophobicity of the N-terminal part is proposed as a measure of the peptide propensity to exhibit hemolytic and other unwanted cytotoxic activities. Based on the information acquired, a rational approach for selective removal of these properties in AMPs is suggested. A proof of concept is gained through engineering specific mutations that resulted in elimination of the hemolytic activity of AMPs (latarcins) while leaving the beneficial antimicrobial effect intact. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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