The potential inhibitory effect of β-casein on the aggregation and deposition of Aβ1-42 fibrils in Alzheimer’s disease: insight from in-vitro and in-silico studies |
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Authors: | Sedighehsadat Hojati Milad Lagzian |
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Institution: | Department of Biology, Faculty of Science, University of Sistan and Baluchestan, Zahedan, Iran |
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Abstract: | Aβ1-40 and Aβ1-42 have been shown to be the main components of the amyloid plaques found in the extracellular environment of neurons in Alzheimer’s disease. β-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 β-casein to suppress the amyloid fibril formation of Aβ1-42 has been examined through in vitro studies and molecular docking simulation. The results demonstrate the inhibitory effect of β-casein on fibril formation in Aβ1-42, in a concentration dependent manner, suggesting that the chaperone binds to the Aβ1-42 and prevents amyloid fibril formation. Molecular docking results show that the inhibitory effect of the β-casein may be due to binding of the chaperone with the aggregation-prone region of the Aβ1-42 mainly via hydrophobic interactions. β-Casein probably binds to the CHC and C-terminal domain of the Aβ1-42, and stabilizes proteins by inhibiting the conversion of monomeric Aβ1-42 into fibrils. Thus our data suggests that the hydrophobic interactions between β-casein and Aβ1-42 play an important role in the burial of the hydrophobic part of the Aβ1-42. This means that β-casein maybe considered for use in preventing amyloid fibril formation in degenerative diseases such as Alzheimer. |
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Keywords: | Alzheimer amyloid fibril chaperone β-casein inhibition molecular dynamics docking |
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