二硫键连接性对 tachyplesin I 结构和抗菌活性的影响。

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

机构信息

Key Laboratory of Marine Drugs, Chinese Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao, 266003, China.

Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266003, China.

出版信息

J Pept Sci. 2018 Jun;24(6):e3087. doi: 10.1002/psc.3087.

DOI:10.1002/psc.3087

PMID:29870123

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.

摘要

肤缩多肤 I 是一种具有广谱抗菌活性的强效抗菌肽。它有 2 个二硫键，可以形成 3 种二硫键异构体。在这项研究中，使用分子动力学模拟、圆二色性结构研究以及抗菌活性和溶血试验，研究了 3 种肤缩多肤 I 异构体（肤缩多肤 I、3C12C、3C7C）的结构和抗菌活性。我们的结果表明，与天然肽相比，这两种异构体（3C12C、3C7C）在结构和活性上有很大的差异。天然肽呈带状构象，而 3C12C 和 3C7C 具有明显不同的二级结构，分别称为“球形”和“珠状”异构体。这两种异构体的溶血作用显著降低，同时抗革兰氏阳性菌活性也显著降低。