Cassia tora Linn.: A boon to Alzheimer's disease for its anti-amyloidogenic and cholinergic activities

BackgroundDrug discovery from natural products as alternatives for Alzheimer's disease (AD) is a current trend. For which plant is an alternative for searching potential molecule for treating AD. Availability of Cassia tora as weed and abundance in nature makes it as potential source. Many plants group under Leguminosae family has potential medicinal property of which Cassia tora is an appropriate choice, to know potency against AD. Etiology of AD is described by senile plaques and neurofibrillary tangles. The Aβ42 has key major role in forming plaques by forming structures like protobirils, oligomers and final fibrilar like structures. Even at in vitro conditions, the peptides have a fibrilar like structure, which was exploited to preliminary screening of natural sources that may be effective in treating AD.Hypothesis/purposeThe design of the study was to unravel the potential medicinal property of Cassia tora for its antioxidant, cholinergic and aggregation inhibition activity.Study designWe evidenced that the methanol (MeOH), n-hexane (n-hex), petroleum ether (PE) and aqueous (aq) extracts from the leaves of Cassia tora (C. tora) were investigated for their inhibitory activity against acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and anti-amyloidogenic assays. The antioxidant effect using 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging, total phenolic and flavonoid contents of the extracts were determined using Folin-Ciocaltaeu's and aluminum chloride (AlCl3) reagents, respectively.ResultsThe methanol extract of C. tora exerted the highest inhibition against AChE (55.38 ± 2.28%) and BChE inhibition (50.02 ± 0.79%) at 100 µg/ml concentration. The methanol extract was also found more active in the antioxidant test. The aggregation kinetics was monitored using thioflavin-T (ThT) assay and transmission electron microscopy (TEM) technique.ConclusionThe results showed that C. tora methanol extract is able to inhibit the Aβ42 aggregation from monomers and oligomers and also able to dis-aggregate the pre-formed fibrils. The study provides an insight on finding new natural products for AD therapeutics.

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