期刊
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 36, 期 8, 页码 2118-2130出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2017.1345326
关键词
Alzheimer; amyloid fibril; chaperone; -casein; inhibition; molecular dynamics; docking
A(1-40) and A(1-42) have been shown to be the main components of the amyloid plaques found in the extracellular environment of neurons in Alzheimer's disease. -Casein, a milk protein, has been shown to display a remarkable chaperone ability in preventing the aggregation of proteins. In this study, the ability of -casein to suppress the amyloid fibril formation of A(1-42) has been examined through in vitro studies and molecular docking simulation. The results demonstrate the inhibitory effect of -casein on fibril formation in A(1-42), in a concentration dependent manner, suggesting that the chaperone binds to the A(1-42) and prevents amyloid fibril formation. Molecular docking results show that the inhibitory effect of the -casein may be due to binding of the chaperone with the aggregation-prone region of the A(1-42) mainly via hydrophobic interactions. -Casein probably binds to the CHC and C-terminal domain of the A(1-42,) and stabilizes proteins by inhibiting the conversion of monomeric A(1-42) into fibrils. Thus our data suggests that the hydrophobic interactions between -casein and A(1-42) play an important role in the burial of the hydrophobic part of the A(1-42.) This means that -casein maybe considered for use in preventing amyloid fibril formation in degenerative diseases such as Alzheimer.
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