Gene set enrichment analysis of α-amylase and α-glucosidase inhibitors of Cassia glauca

Background The present study aimed to evaluate in vitro α-amylase and α-glucosidase inhibitory activity of various extracts of Cassia glauca, predict the binding affinity of multiple phytoconstituents with both enzymes via in silico molecular docking and identify the probably modulated pathways by t...

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Bibliographic Details
Published inJournal of diabetes and metabolic disorders Vol. 19; no. 2; pp. 683 - 689
Main Authors Ternikar, Shama G, Patil, MB, Pasha, Ismail, Khanal, Pukar
Format Journal Article
LanguageEnglish
Published Cham Springer International Publishing 01.12.2020
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Summary:Background The present study aimed to evaluate in vitro α-amylase and α-glucosidase inhibitory activity of various extracts of Cassia glauca, predict the binding affinity of multiple phytoconstituents with both enzymes via in silico molecular docking and identify the probably modulated pathways by the lead hit. Methods Different extracts of Cassia glauca i.e. acetone, ethanol, and aqueous extracts were evaluated for α-amylase and α-glucosidase inhibitory activity using in vitro method in which starch and 4-Nitrophenyl β-D-glucopyranoside were used as substrate respectively. Similarly, the docking study was performed using autodock4 to predict the binding affinity of phytoconstituents with α-amylase and α-glucosidase. After docking, ten different poses were obtained for the ligand molecule. Among them, the pose of ligand molecule with the lowest binding energy was visualized in Discovery Studio 2019. Results and conclusion Among the multiple extracts, the aqueous extract showed the highest α-amylase (IC 50 :652.10 ± 20.09) and α-glucosidase (IC 50 :482.46 ± 8.70) inhibitory activity. Similarly, cassiaoccidentalin B was predicted to have the highest binding affinity with both enzymes. The potency of aqueous extract to inhibit α-amylase and α-glucosidase could be due to multiple water-soluble compounds like saponins, flavonoids, and glycosides.
ISSN:2251-6581
2251-6581
DOI:10.1007/s40200-020-00538-9