Alzheimer’s disease (AD) progresses due to beta amyloid aggregation and decreased acetylcholine level. Amyloid-β peptide (Aβ) formed by the continuous proteolytic processing of β-amyloid precursor protein (β APP) by β-secretase (BACE1) and γ-secretase (BACE2), plays a vital role in the pathogenesis of Alzheimer’s disease (AD). Evaluated dipeptides and heterocyclic fused dipeptide derivative exhibit inhibitory action against acetyl cholinesterase enzyme. In-silico docking analysis for dipeptides and heterocyclic fused dipeptide was carried out using GLIDE software. The docking score of DP IV and DPI was found to be -7.63 and -7.08 and the standard donepezil (AChE inhibitor) showed docking score of -4.97 using GLIDE against AChE. In-vitro enzyme inhibition assay was carried out for AChE enzyme and the IC50 value of DP IV was found to be 0.399 μg/ml and the standard donepezil (AChE inhibitor) was found to be 0.065 μg/ml. Based on the results obtained from in-silico docking studies and in-vitro enzyme inhibition, both are correlated with each other.
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