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N‐terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: A case study in latarcins
Author(s) -
Polyansky Anton A.,
Vassilevski Alexander A.,
Volynsky Pavel E.,
Vorontsova Olga V.,
Samsonova Olga V.,
Egorova Natalya S.,
Krylov Nicolay A.,
Feofanov Alexei V.,
Arseniev Alexander S.,
Grishin Eugene V.,
Efremov Roman G.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.044
Subject(s) - antimicrobial peptides , amphiphile , antimicrobial , peptide , in silico , chemistry , biochemistry , biology , microbiology and biotechnology , gene , organic chemistry , copolymer , polymer
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.