PAP248-286缩氨酸寡聚的原子模拟

IF 0.4 Q4 MULTIDISCIPLINARY SCIENCES Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki Pub Date : 2022-01-01 DOI:10.26907/2542-064x.2022.2.185-195

A. O. Nikitina, A. Yulmetov, A. Kusova, V. Klochkov, D. S. Blokhin

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引用次数: 0

摘要

淀粉样蛋白原纤维是各种可溶性蛋白和多肽的有序聚集体。淀粉样蛋白原纤维与20多种人类疾病有关，包括阿尔茨海默氏症、帕金森症、亨廷顿舞蹈症和艾滋病毒感染。某些蛋白与纤维结构形成的关联是淀粉样蛋白疾病病理表现的特征。澄清淀粉样蛋白原纤维形成的物理化学参数对我们理解和后续治疗淀粉样蛋白疾病至关重要。目前对功能性多肽和致病性多肽的自组装机制进行了全面的研究。肽

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Atomistic Simulations of PAP248-286 Peptide Oligomerization

Amyloid fibrils are ordered aggregates that from a wide variety of soluble proteins and peptides. Amyloid fibrils take part into more than 20 human diseases, including Alzheimer’s, Parkinson, Huntington and HIV infection. The association of certain proteins with the fibril structure formation characterizes the pathological manifestation of amyloid diseases. Clarification of the physicochemical parameters of the amyloid fibril formation is critical to our understanding and subsequent treatment of amyloid diseases. There are several comprehensive studies of self-assembly mechanisms of functional and pathogenic polypeptides. peptide

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