Phytochemical Profile, Antioxidant, α-amylase Inhibition, Binding Interaction and Docking Studies of Justicia carnea Bioactive Compounds with α-amylase
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Date
2021
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ELSEVIER Biophysical Chemistry
Abstract
The present study investigated the antioxidant and in vitro antidiabetic capacities of Justicia
carnea aqueous leaf extract (JCAE) using α-amylase inhibition model. α-Amylase binding-interaction
with JCAE was also investigated using fluorescence spectroscopy and molecular docking. Phytochemical
screening and Gas ChromatographyMass Spectrometry (GC–MS) analysis indicated presence of bioactive
compounds. Phenolic (132 mg GAE/g) and flavonoid contents (31.08 mg CE/g) were high. JCAE exhibited
high antioxidant capacity and effectively inhibited α-amylase activity (IC50, 671.43 ± 1.88 μg/mL),
though lesser than acarbose effect (IC50, 108.91 ± 0.61 μg/mL). α-Amylase intrinsic fluorescence was
quenched in the presence of JCAE. Ultraviolet-visible and FTIR spectroscopies affirmed mild changes in
α-amylase conformation. Synchronous fluorescence analysis indicated alterations in the
microenvironments of tryptophan residues near α-amylase active site. Molecular docking affirmed non polar interactions of compounds 6 and 7 in JCAE with Asp-197 and Trp-58 residues of α-amylase,
respectively. Overall, JCAE indicated potential to prevent postprandial hyperglycemia by slowing down
carbohydrate hydrolysis
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Keywords
Justicia carnea, α-Amylase inhibition, Antioxidant, Binding interaction, Fluorescence quenching, Molecular docking