Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050110 | FEBS Letters | 2009 | 4 Pages |
Abstract
In silico structural analyses of sets of α-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.
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Authors
Anton A. Polyansky, Alexander A. Vassilevski, Pavel E. Volynsky, Olga V. Vorontsova, Olga V. Samsonova, Natalya S. Egorova, Nicolay A. Krylov, Alexei V. Feofanov, Alexander S. Arseniev, Eugene V. Grishin, Roman G. Efremov,