2026-05-20T14:06:57Z https://www.peertechzpublications.org/oai-pmh

oai:www.peertechzpublications.org:10.17352/ijcem.000024 2017-07-08 PTZ.IJCEM:VOL3

Dipeptidyl Peptidase IV Inhibitory Activity of Berberine and Mangiferin: An In Silico Approach Ipseeta Ray Mohanty Selvaa KumarRajesh Suman<p><strong>Background:</strong> Dipeptidyl peptidase-IV (DDP-IV) Inhibitors may represent single anti-diabetic drugs, the multiple actions of which may translate into demonstrable therapeutic benefits in&nbsp;&nbsp; diabetes. The marketed synthetic DPP-IV Inhibitors are expensive drugs and have been reported to cause unacceptable adverse effects&nbsp; such&nbsp; as&nbsp; pancreatitis,&nbsp; angioedema,&nbsp; thyroid&nbsp; and&nbsp; pancreatic&nbsp; cancers.&nbsp; In&nbsp; this&nbsp; scenario,&nbsp; research&nbsp; to&nbsp; identify DPP-IV Inhibitors from alternative sources is desirable. <br></p><p><strong>Aims and Objective: </strong>The study was designed to elucidate the DPP-IV Inhibitory activity of Berberine and Mangiferin, determine the binding sites and affinity of Berberine and Mangiferin for DPP- IV enzyme using in silico studies and compare it to synthetic DPP-IV Inhibitor: Vildagliptin. <br></p><p><strong>Material&nbsp; and&nbsp; Methods:</strong> The&nbsp; crystal&nbsp; structure&nbsp; of&nbsp; human&nbsp; DPP&nbsp; IV&nbsp; (PDB&nbsp; Id:&nbsp; 2QT9)&nbsp; was&nbsp; downloaded&nbsp; from Protein Databank. Berberine and Mangiferin were computationally designed and screened through in silico docking&nbsp; studies&nbsp; against&nbsp; crystal&nbsp; structure&nbsp; of&nbsp; DP-IV.&nbsp; Computational&nbsp; in&nbsp; silico studies&nbsp; were&nbsp; used&nbsp; to&nbsp; identify&nbsp; the&nbsp; sites&nbsp; as&nbsp; well&nbsp; as&nbsp; amino&nbsp; acid&nbsp; residues&nbsp; on&nbsp; DPP-IV&nbsp; enzyme&nbsp; to&nbsp; which&nbsp; these&nbsp; natural&nbsp; DPP-IV&nbsp; Inhibitors binds.&nbsp; <br></p><p><strong>Results:</strong> The&nbsp; DPP-IV&nbsp; Inhibitory&nbsp; activity&nbsp; of&nbsp; Mangiferin&nbsp; was&nbsp; found&nbsp; to&nbsp; be&nbsp; comparable&nbsp; to&nbsp; synthetic&nbsp; marketed DPP-IV Inhibitors; Vildagliptin and Sitagliptin. Like Vildagliptin, Berberine and Mangiferin bind within the active site pocket (the 1st largest pocket) of DPP-IV enzyme whereas, Sitagliptin prefers to bind in the second largest pocket of DPP-IV enzyme. Berberine prefers to bind to the active site pocket of DPP-IV enzyme. Berberine binds very close to Glu205 and Glu206. As delineated using in silico binding energy results, Mangiferin, possess superior DPP-IV inhibitory activity as compared to Sitagliptin and Vildagliptin. &nbsp;</p><p><strong>Conclusion:</strong> In silico studies demonstrates that Berberine and Mangiferin possess significant DPP-IV Inhibitory activity comparable to marketed synthetic DPP-IV Inhibitors.</p> International Journal of Clinical Endocrinology and Metabolism - Peertechz Publications 2017-07-08 Research Article https://doi.org/10.17352/ijcem.000024 en Copyright © Ipseeta Ray Mohanty et al.