基于密度泛函理论的四种 Aβ42 纤维状构象的拓扑结构分析。
A DFT-Assisted Topological Analysis of Four Polymorphic, S-Shaped Aβ42 Fibril Structures.
机构信息
Department of Chemistry and Biochemistry, University of California Santa Cruz, Physical Science Building 356, 1156 High Street, Santa Cruz, CA, 95064, USA.
出版信息
Chembiochem. 2019 Jul 1;20(13):1722-1724. doi: 10.1002/cbic.201900036. Epub 2019 May 21.
Amyloid β 42 (Aβ42) is an inherently disordered peptide, whose toxic actions are believed to play important roles in the etiology of Alzheimer's disease. Four fibril structures of the peptide that display broadly similar characteristics were recently published, but a systematic comparison of these structures is lacking. In this paper, a topological framework was created to enable such understanding and produced new insights into subtle structural elements that underlie the overall structural diversity. A DFT-based analysis illuminated some of the energetic differences that arise as a consequence.
淀粉样蛋白 β 42（Aβ42）是一种固有无序的肽，其毒性作用被认为在阿尔茨海默病的发病机制中发挥着重要作用。最近发表了该肽的四种纤维结构，它们具有广泛相似的特征，但这些结构之间缺乏系统的比较。在本文中，创建了一个拓扑框架来实现这种理解，并深入了解了导致整体结构多样性的细微结构元素。基于密度泛函理论的分析阐明了由此产生的一些能量差异。
Zotero 插件