Background: Dipeptidyl peptidase-IV (DDP-IV) Inhibitors may represent single anti-diabetic drugs, the multiple actions of which may translate into demonstrable therapeutic benefits in diabetes. The marketed synthetic DPP-IV Inhibitors are expensive drugs and have been reported to cause unacceptable adverse effects such as pancreatitis, angioedema, thyroid and pancreatic cancers. In this scenario, research to identify DPP-IV Inhibitors from alternative sources is desirable.
Aims and Objective: 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.
Material and Methods: The crystal structure of human DPP IV (PDB Id: 2QT9) was downloaded from Protein Databank. Berberine and Mangiferin were computationally designed and screened through in silico docking studies against crystal structure of DP-IV. Computational in silico studies were used to identify the sites as well as amino acid residues on DPP-IV enzyme to which these natural DPP-IV Inhibitors binds.
Results: The DPP-IV Inhibitory activity of Mangiferin was found to be comparable to synthetic 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.
Conclusion: In silico studies demonstrates that Berberine and Mangiferin possess significant DPP-IV Inhibitory activity comparable to marketed synthetic DPP-IV Inhibitors.
Keywords: Berberine, Mangiferin; Sitagliptin; Vilda-gliptin; in silico and DPP-IV
Published on: Jul 8, 2017 Pages: 18-22
Full Text PDF
Full Text HTML
DOI: 10.17352/ijcem.000024
CrossMark
Publons
Harvard Library HOLLIS
Search IT
Semantic Scholar
Get Citation
Base Search
Scilit
OAI-PMH
ResearchGate
Academic Microsoft
GrowKudos
Universite de Paris
UW Libraries
SJSU King Library
SJSU King Library
NUS Library
McGill
DET KGL BIBLiOTEK
JCU Discovery
Universidad De Lima
WorldCat
VU on WorldCat
PTZ: We're glad you're here. Please click "create a new query" if you are a new visitor to our website and need further information from us.
If you are already a member of our network and need to keep track of any developments regarding a question you have already submitted, click "take me to my Query."