Secondary Metabolite Profiling, Antioxidant, Antidiabetic and Neuroprotective Activity of Cestrum nocturnum (Night Scented-Jasmine): Use of In Vitro and In Silico Approach in Determining the Potential Bioactive Compound

This study aims to describe the therapeutic potential of C. nocturnum leaf extracts against diabetes and neurological disorders via the targeting of alpha-amylase and acetylcholinesterase (AChE) activities, followed by computational molecular docking studies to establish a strong rationale behind the alpha-amylase and AChE inhibitory potential of C. nocturnum leaves-derived secondary metabolites. In our study, the antioxidant activity of the sequentially extracted C. nocturnum leaves extract was also investigated, in which the methanolic fraction exhibited the strongest antioxidant potential against DPPH (IC50 39.12 +/- 0.53 mu g/mL) and ABTS (IC50 20.94 +/- 0.82 mu g/mL) radicals. This extract strongly inhibited the alpha-amylase (IC(50)188.77 +/- 1.67 mu g/mL) and AChE (IC50 239.44 +/- 0.93 mu g/mL) in a non-competitive and competitive manner, respectively. Furthermore, in silico analysis of compounds identified in the methanolic extract of the leaves of C. nocturnum using GC-MS revealed high-affinity binding of these compounds with the catalytic sites of alpha-amylase and AChE, with binding energy ranging from -3.10 to -6.23 kcal/mol and from -3.32 to -8.76 kcal/mol, respectively. Conclusively, the antioxidant, antidiabetic, and anti-Alzheimer activity of this extract might be driven by the synergistic effect of these bioactive phytoconstituents.

Automated summary

This study aims to investigate the therapeutic potential of C. nocturnum leaf extracts against diabetes and neurological disorders through inhibitory activities on alpha-amylase and acetylcholinesterase (AChE). Computational molecular docking studies support the inhibitory potential of C. nocturnum leaves-derived secondary metabolites on alpha-amylase and AChE. The methanolic fraction of the leaf extract showed strong antioxidant activity and inhibited alpha-amylase and AChE in a non-competitive and competitive manner, respectively. In silico analysis revealed high-affinity binding of compounds in the methanolic extract to the active sites of alpha-amylase and AChE.