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Virtual Screening of Dipeptidyl Peptidase IV Inhibitors from Zinc Database
| International Journal of Computer Applications |
| Foundation of Computer Science (FCS), NY, USA |
| Volume 56 - Number 8 |
| Year of Publication: 2012 |
| Authors: Phani Kumar Yadla, Allam Appa Rao, A. Swaroopa Rani, M. Naresh Babu |
10.5120/8912-2959
|
Phani Kumar Yadla, Allam Appa Rao, A. Swaroopa Rani, M. Naresh Babu . Virtual Screening of Dipeptidyl Peptidase IV Inhibitors from Zinc Database. International Journal of Computer Applications. 56, 8 ( October 2012), 31-34. DOI=10.5120/8912-2959
Abstract
Dipeptidyl peptidase IV (DPP IV) is a serine exopeptidase that cleaves X-proline dipeptides from the N terminus of polypeptides. Dipeptidyl peptidase IV enzyme activity has been implicated in the regulation of the biological activity of multiple hormones and chemokines, including the insulinotropic peptides glucagon-like peptide-1 (GLP1) and glucose-dependent insulinotropic polypeptide (GIP). Hence, DPP IV has an important role in glucose homeostasis, and was established as a potential target for therapy in type II diabetes. Hence, there is a need to identify the most potent compound that would specifically target DPP IV. Initially, protein structure DPP IV was extracted from Protein Data Bank by performing a search resulted in 86 hits. They are filtered based on the presence of X-ray diffraction as the experimental method, between 2. 0 and 2. 5 Aº resolution and with bound ligands. From the result, presence of breaks in the protein are checked and based on Ramchandran plot, 2QOE was selected as the protein target. Further analysis was carried to screen compounds from ZINC database, on Lipinski's rule of 5 using the virtual screening software like eHiTS.
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