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Reduction of Helical Content by Insertion of a Disulfide Bond Leads to an Antimicrobial Peptide with Decreased Hemolytic Activity
Author(s) -
Hwang Heeyong,
Hyun Soonsil,
Kim Yangsoo,
Yu Jaehoon
Publication year - 2013
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201200463
Subject(s) - disulfide bond , antimicrobial , intramolecular force , peptide , amphiphile , chemistry , cationic polymerization , combinatorial chemistry , mutant , stereochemistry , biochemistry , organic chemistry , copolymer , gene , polymer
CAPs off to the S–S bond: Application of a strategy involving the introduction of intramolecular disulfide bonds to amphipathic cationic antimicrobial peptides (CAPs) led to decreased α‐helicity and hydrophobicity. The mutant peptides were observed to have significantly increased (250‐fold) minimum hemolytic concentrations while maintaining MIC values against E. coli , affording more therapeutically selective CAPs.