Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/79206
Title: Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I
Authors: Shi, J
So, LY 
Chen, FL
Liang, JZ
Chow, HY 
Wong, KY 
Wan, SB
Jiang, T
Yu, RL
Keywords: Antimicrobial activity
Antimicrobial peptide
Disulfide connectivity
Secondary structure
Tachyplesin I
Issue Date: 2018
Publisher: John Wiley & Sons Ltd.
Source: Journal of peptide science, June 2018, v. 24, no. 6, UNSP e3087 How to cite?
Journal: Journal of peptide science 
Abstract: 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.
URI: http://hdl.handle.net/10397/79206
ISSN: 1075-2617
EISSN: 1099-1387
DOI: 10.1002/psc.3087
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