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  • Title: N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins.
    Author: Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG.
    Journal: FEBS Lett; 2009 Jul 21; 583(14):2425-8. PubMed ID: 19563807.
    Abstract:
    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.
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