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Biophys Chem ; 269: 106529, 2021 02.
Article in English | MEDLINE | ID: mdl-33360111

ABSTRACT

The present study investigated the antioxidant and invitro 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 Chromatography-Mass 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 FT-IR 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.


Subject(s)
Justicia/chemistry , Molecular Docking Simulation , Phytochemicals/chemistry , Phytochemicals/pharmacology , alpha-Amylases/antagonists & inhibitors , alpha-Amylases/metabolism , Antioxidants/chemistry , Antioxidants/metabolism , Antioxidants/pharmacology , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/metabolism , Enzyme Inhibitors/pharmacology , Phytochemicals/metabolism , Protein Conformation , Spectroscopy, Fourier Transform Infrared , alpha-Amylases/chemistry
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