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在朊病毒和淀粉样蛋白结构对折叠环境的依赖性上。

On the Dependence of Prion and Amyloid Structure on the Folding Environment.

机构信息

Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, 31-034 Kopernika 7, 30-688 Krakow, Poland.

Department of Applied Informatics, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland.

出版信息

Int J Mol Sci. 2021 Dec 16;22(24):13494. doi: 10.3390/ijms222413494.

DOI:10.3390/ijms222413494
PMID:34948291
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8707753/
Abstract

Currently available analyses of amyloid proteins reveal the necessity of the existence of radical structural changes in amyloid transformation processes. The analysis carried out in this paper based on the model called fuzzy oil drop (FOD) and its modified form (FOD-M) allows quantifying the role of the environment, particularly including the aquatic environment. The starting point and basis for the present presentation is the statement about the presence of two fundamentally different methods of organizing polypeptides into ordered conformations-globular proteins and amyloids. The present study shows the source of the differences between these two paths resulting from the specificity of the external force field coming from the environment, including the aquatic and hydrophobic one. The water environment expressed in the fuzzy oil drop model using the 3D Gauss function directs the folding process towards the construction of a micelle-like system with a hydrophobic core in the central part and the exposure of polarity on the surface. The hydrophobicity distribution of membrane proteins has the opposite characteristic: Exposure of hydrophobicity at the surface of the membrane protein with an often polar center (as in the case of ion channels) is expected. The structure of most proteins is influenced by a more or less modified force field generated by water through the appropriate presence of a non-polar (membrane-like) environment. The determination of the proportion of a factor different from polar water enables the assessment of the protein status by indicating factors favoring the structure it represents.

摘要

目前对淀粉样蛋白的分析揭示了在淀粉样转化过程中存在激进结构变化的必要性。本文基于模糊油滴（FOD）模型及其修正形式（FOD-M）进行的分析，允许量化环境的作用，特别是包括水相环境。本研究的出发点和基础是关于存在两种将多肽组织成有序构象的根本不同方法的陈述 - 球状蛋白和淀粉样蛋白。本研究表明，这两种途径之间的差异的根源是来自环境的外部力场的特异性，包括水相和疏水性。在使用 3D 高斯函数的模糊油滴模型中表达的水环境将折叠过程引导到构建具有疏水性核心的胶束样系统中，在中心部分和表面暴露极性。膜蛋白的疏水性分布具有相反的特征：预期在膜蛋白的表面暴露疏水性，其中心通常具有极性（如离子通道的情况）。大多数蛋白质的结构受到或多或少由水通过适当存在非极性（膜样）环境产生的力场的影响。通过确定不同于极性水的因素的比例，可以通过指示有利于它所代表的结构的因素来评估蛋白质的状态。

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