The potential inhibitory effect of β-casein on the aggregation and deposition of Aβ fibrils in Alzheimer's disease: insight from in-vitro and in-silico studies.

Aβ and Aβ 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 Aβ has been examined through in vitro studies and molecular docking simulation. The results demonstrate the inhibitory effect of β-casein on fibril formation in Aβ, in a concentration dependent manner, suggesting that the chaperone binds to the Aβ 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 Aβ mainly via hydrophobic interactions. β-Casein probably binds to the CHC and C-terminal domain of the Aβ and stabilizes proteins by inhibiting the conversion of monomeric Aβ into fibrils. Thus our data suggests that the hydrophobic interactions between β-casein and Aβ play an important role in the burial of the hydrophobic part of the Aβ This means that β-casein maybe considered for use in preventing amyloid fibril formation in degenerative diseases such as Alzheimer.