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Computational studies of dipeptidyl peptidase IV inhibitors
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Medicinal Chemistry

ISSN: 2161-0444

Open Access

Computational studies of dipeptidyl peptidase IV inhibitors


4th International Conference on Medicinal Chemistry & Computer Aided Drug Designing

November 02-04, 2015 Atlanta, USA

Dhruti Patel, Jagat Upadhyay, Tejas Patel and B N Suhagia

Dharmsinh Desai University, India

Posters-Accepted Abstracts: Med chem

Abstract :

Diabetes is an illness characterized by abnormally high level of glucose in blood. Type 2 diabetes (T2D) is one of the major concerns for the health of individual around the World in 21st century as the prevalence of diabetes is increased apace. Dipeptidyl Peptidase IV (DPP IV) inhibitors are relatively new therapy for management of T2D. Inhibition of DPP-IV is an attractive new approach to the management of type 2 diabetes. DPP IV belongs to a family of prolyl-specific proteases that consists of several closely related enzymes in family: DPP-2/QPP, DPP-8, DPP-9, FAP-�±. DPP IV is a highly specific serine aminoprotease that preferentially cleaves oligopeptides. It cleaves peptide from N-terminal where penultimate (P1) amino acid is either alanine or proline. X-ray crystal structure of DPP IV is solved in na�¯ve form and inhibitor bound form. Around 85 solved crystal structures have been deposited to Protein Data Bank by different research groups till date. DPP IV inhibitors reported till date are chemically very diverse indicating that they may bind differently to active site of DPP IV. To understand binding mode of DPP IV inhibitors, diverse inhibitors were docked into active site of DPP IV. Result of the study revealed that vildagliptin and saxagliptin bind to unprimed S1 and S2 subsite of enzyme active site. Sitagliptin, teneligliptin, omarigliptin, carmegliptin, gosoglipitn and anagliptin binds to S2 extensive site in addition to S1 and S2 subsite. Alogliptin and imigliptin binds to primed S1â�� site in addition to S1 and S2 subsite. Linaglipitn occupies S1â��, S2â�� as well as S1 and S2 subsites. DPP IV inhibition tends to increase with increase in number of binding sites. All DPP IV inhibitors make important hydrophobic interaction with S1 subsite and salt bridge interactions with GLU205 and/ or GLU206 motif.

Biography :

Dhruti Patel is Postgraduate student in Pharmaceutical Science at Faculty of Pharmacy, Dharmsinh Desai University, Nadiad, Guajrat, India. She is doing her project work on Drug Designing using CADD.

Email: dhruti.patel317@gmail.com

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Citations: 6627

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