IN-SILICO SCRUTINY AND MOLECULAR DOCKING ANALYSIS FOR BETA SECRETASE-1 AND PRESENILIN-1

Abstract

We have performed comparative scrutiny between the canonical and non-canonical isoforms of beta secretase-1 and presenilin-1 by various bioinformatics tools for understanding the disparities existent among them. Conjointly, the PDB structure of these neural proteins were docked with two therapeutic drugs (bexarotene and hesperidin) and a toxin (streptozotocin). Results: In-silico scrutiny revealed consanguinity among beta secretase-1 isoforms. On the contrary, amongst presenilin-1 isoforms significant disparities were observed. Molecular docking predicted ubieties of bexarotene, hesperidin and streptozotocin binding sites on beta secretase-1 and presenilin-1. Conclusion: The study propounds pernicious effect of streptozotocin on essential neural proteins and therapeutic potential of bexarotene and hesperidin in Alzheimer’s disease and other neurodegenerative disorders. Additionally, the study raises a strong need for evaluation of functionalities of non-canonical isoforms of beta secretase-1 and presenilin-1, in order to uncover their roles in the pathogenesis of Alzheimer's disease and other neurodegenerative disorders.