Phytochemical Profile, Antioxidant, α-amylase Inhibition, Binding Interaction and Docking Studies of Justicia carnea Bioactive Compounds with α-amylase

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dc.contributor.authorAvwioroko, Oghenetega
dc.date.accessioned2022-09-15T12:16:34Z
dc.date.available2022-09-15T12:16:34Z
dc.date.issued2021
dc.description.abstractThe 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 hydrolysisen_US
dc.identifier.issnhttps://doi.org/10.1016/j.bpc.2020.106529
dc.identifier.urihttp://dspace.run.edu.ng:8080/jspui/handle/123456789/3642
dc.language.isoenen_US
dc.publisherELSEVIER Biophysical Chemistryen_US
dc.subjectJusticia carneaen_US
dc.subjectα-Amylase inhibitionen_US
dc.subjectAntioxidanten_US
dc.subjectBinding interactionen_US
dc.subjectFluorescence quenchingen_US
dc.subjectMolecular dockingen_US
dc.titlePhytochemical Profile, Antioxidant, α-amylase Inhibition, Binding Interaction and Docking Studies of Justicia carnea Bioactive Compounds with α-amylaseen_US
dc.typeArticleen_US
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