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Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I
Author(s) -
Shi Juan,
So LokYan,
Chen Fangling,
Liang Jiazhen,
Chow HoYin,
Wong KwokYin,
Wan Shengbiao,
Jiang Tao,
Yu Rilei
Publication year - 2018
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3087
Subject(s) - antimicrobial , circular dichroism , chemistry , peptide , disulfide bond , hemolysis , stereochemistry , antimicrobial peptides , biochemistry , organic chemistry , biology , immunology
Tachyplesin I is a potent antimicrobial peptide with broad spectrum of antimicrobial activity. It has 2 disulfide bonds and can form 3 disulfide bond isomers. In this study, the structure and antimicrobial activity of 3 tachyplesin I isomers (tachyplesin I, 3C12C, 3C7C) were investigated using molecular dynamic simulations, circular dichroism structural study, as well as antimicrobial activity and hemolysis assay. Our results suggest that in comparison to the native peptide, the 2 isomers (3C12C, 3C7C) have substantial structural and activity variations. The native peptide is in the ribbon conformation, while 3C12C and 3C7C possess remarkably different secondary structures, which are referred as “globular” and “beads” isomers, respectively. The substantially decreased hemolysis effects for these 2 isomers is accompanied by significantly decreased anti‐gram‐positive bacterial activity.