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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Mechanism of beta-purothionin antimicrobial peptide inhibition by metal ions: Molecular dynamics simulation study
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Mechanism of beta-purothionin antimicrobial peptide inhibition by metal ions: Molecular dynamics simulation study

机译:金属离子抑制β-硫氧磷蛋白抗菌肽的机理:分子动力学模拟研究

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摘要

Wheat beta-purothionin is a highly potent antimicrobial peptide which, however, is inactivated by metal ions. The key structural properties and mechanisms of inhibition of beta-purothionin were investigated for the first time using unconstrained molecular dynamics simulations in explicit water. A series of simulations were performed to determine effects of temperature and the metal ions. Analyses of the unconstrained simulations allowed the experimentally unavailable structural and dynamic details to be unambiguously examined. The global fold and the alpha 1 helix of beta-purothionin are thermally stable and not affected by metal ions. In contrast, the alpha 2 helix unfolds with shift of temperature from 300 K and in the presence of metal ions. The network of conserved residues including Arg30 and Lys5 is sensitive to environmental changes and triggers unfolding. Loop regions display high flexibility and elevated dynamics, but are affected by metal ions. Our study provides insights into the mechanism of metal ion-based inhibition. (c) 2005 Elsevier B.V. All rights reserved.
机译:小麦β-硫氧磷蛋白是一种高效的抗菌肽,但是被金属离子灭活。使用显性水中的无约束分子动力学模拟,首次研究了关键的结构性质和抑制β-硫氧磷的机理。进行了一系列模拟以确定温度和金属离子的影响。通过对无限制仿真的分析,可以明确检查实验上不可用的结构和动态细节。 β-purothionin的全局折叠和α1螺旋是热稳定的,不受金属离子的影响。相反,随着温度从300 K开始变化并且存在金属离子,α2螺旋会展开。包括Arg30和Lys5在内的保守残基网络对环境变化敏感并触发展开。环状区域显示出较高的柔韧性和较高的动力学性能,但会受到金属离子的影响。我们的研究提供了对基于金属离子的抑制机理的见解。 (c)2005 Elsevier B.V.保留所有权利。

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