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A β 42 and A β 40: similarities and differences
Author(s) -
Qiu Tian,
Liu Qian,
Chen YongXiang,
Zhao YuFen,
Li YanMei
Publication year - 2015
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2789
Subject(s) - proteolysis , gene isoform , amyloid (mycology) , mechanism (biology) , biochemistry , disease , peptide , alzheimer's disease , chemistry , biology , neuroscience , medicine , gene , enzyme , inorganic chemistry , philosophy , epistemology
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.