In Silico Analysis of Baicalin’s Binding on Amyloid- β, Presenilin-1 and Tau Proteins: Validation in a Mouse Model of Cerebral Amyloidosis |Biomedgrid

The production of amyloid-β following activation of presenilin-1 and accumulation of the hyperphosphorylated tau protein contribute to Alzheimer's disease development. In order to understand Baicalin's effect on AD treatment, we have used in silico studies to predict its binding on amyloid-β, presenilin-1 and tau protein receptors. Computational molecular docking was performed using Molegro Virtual Docker software. The scores obtained were -112.35, -68 and -53 Kcal/mol respectively for the three receptors, indicating potent inhibitory effect of Baicalin on amyloid-β (highest binding score). Moreover, Baicalin showed high affinity towards 3jq5 (amyloid-β protein receptor) as it showed thirteen hydrogen bonds with nine amino acids. Contrary to what was observed with amyloid-β, a lower binding affinity was observed for tau-protein. In addition, to confirm molecular docking results, in vivo studies using APP/PS1 mice (a model of cerebral amyloidosis) treatment with Baicalin showed that it restores behavioural impairment, inhibits the production of amyloid-β in the cortex, alongside with the inhibition of macrophage infiltration in the brains of these mice. These findings open new ways for deeper understanding of the amyloid hypothesis in AD and consideration of Baicalin as a promising drug for AD treatment.