Effect of disulfide bridges deletion on the conformation of the androctonin,polyphemusin-I,and thanatin antimicrobial peptides:molecular dynamics simulation studies

作     者：Jorge Ricardo Moreira Castro Carlos Alessando Fuzo Leo Degreve 

作者机构：Grupo de Simulacao MolecularFaculdade de Filosofia Ciencias e Letras de Ribeirao PretoUniversidade de Sao PauloRibeirao PretoBrazil 

出 版 物：《Journal of Biophysical Chemistry》 (生物物理化学（英文）)

年 卷 期：2011年第2卷第3期

页      面：244-257页

学科分类：1002[医学-临床医学] 100214[医学-肿瘤学] 10[医学] 

基　　金：Fundacao de Amparo a Pesquisa do Estado de Sao Paulo(FAPESP)for financial support 

主　　题：Androctonin Polyphemusin-I Thanatin Antimicrobial Peptides Cysteine Rich Peptides Molecular Simulation Disulfide Bridges Deletion 

摘      要：In this work, the role of the disulfide bridges in the maintenance of the secondary structure of the antimicrobial peptides androctonin, poly-phemusin-I, and thanatin is analyzed on the basis of their structural characteristics and of three of their respective mutants, andry4, poly4, and thany2, in which all the cysteine residues have been replaced with tyrosine residues. The absence of the disulfide bridges in andry4, poly4, and thany2 seems to be compensated by an overall enforcement of the original hydrogen bonds and by extra attractive interactions between the aromatic rings of the tyrosine residues. In spite of the mutations, the original β-hairpin structures are maintained in the three mutants, but the best conformational similarities are found for the androctonin/andry4 pair.