蛋白质水解
基因亚型
淀粉样蛋白(真菌学)
机制(生物学)
生物化学
疾病
肽
阿尔茨海默病
化学
生物
神经科学
医学
内科学
基因
酶
无机化学
哲学
认识论
作者
Tian Qiu,Qian Liu,Yong‐Xiang Chen,Yufen Zhao,Yanmei Li
摘要
The abnormal accumulation of amyloid‐ β (A β ) peptide in the brain is one of the most important hallmarks of Alzheimer's disease. A β is an aggregation‐prone and toxic polypeptide with 39–43 residues, derived from the amyloid precursor protein proteolysis process. According to the amyloid hypothesis, abnormal accumulation of A β in the brain is the primary influence driving Alzheimer's disease pathologies. Among all kinds of A β isoforms, A β 40 and A β 42 are believed to be the most important ones. Although these two kinds of A β differ only in two amino acid residues, recent studies show that they differ significantly in their metabolism, physiological functions, toxicities, and aggregation mechanism. In this review, we mainly summarize the similarities and differences between A β 42 and A β 40, recent studies on selective inhibitors as well as probes will also be mentioned. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.
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