Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I

August 13, 2018

Title

Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I

Author

Juan Shi, Lok‐Yan So, Fangling Chen, Jiazhen Liang, Ho‐Yin Chow, Kwok‐Yin Wong, Shengbiao Wan, Tao Jiang, Rilei Yu

Year

2018

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.

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Chemical stability, Biochemistry