The Docking of Protein DPP4 and Drug Molecules for Type 2 Diabetes
Abstract: DPP 4 inhibitors are emerging as new drugs for type 2 diabetes treatment. In this paper we use molecular docking technology between DPP4 protein and 5 kinds of inhibitors in order to help to understanding the study of new inhibitors. The results showed that the hydrogen bonds are formed between Alogliptin inhibitor and DPP4 at GLU206, TYR662, ARG125; salt bridge is formed at GLU205; there are also hydrogen bond in GLU205, GLU206, TYR662, ARG125 between saxagliptin and Dpp4. Also one hydrogen bonding is formed between the backbone with residue GLU205; Linagliptin formed hydrogen at GLU205, TYR662, ARG125, also formed salt bridge at GLU206 bridge and had Pi-Pi interaction at TUR547; Sitagliptin had hydrogen bond at GLU205 and TYR662, salt bridge at GLU206, and PI-PI interaction at TYR666 during docking process; Vilagliptin formed hydrogen bonds at GLU205D and salt bridge at GLU206.
文章引用: 李恒臻 , 庄立晖 , 刘 哲 , 王晓艳 (2017) 靶向DPP4与2型糖尿病相关药物分子的对接研究。 临床医学进展， 7， 16-22. doi: 10.12677/ACM.2017.71004
 Bonner, W.S. (2000) Life and Death of the Pancreatic Beta Cells. Trends in Endocrinology and Metabolism, 11, 375-378.
Lugari, R., Dei Cas, A., Ugolotti, D., et al. (2002) Evidence for Early Impairment of Glucagon-Like Peptide1-Induced insulin Secretion in Human Type 2 (Non Insulin-Dependent) Diabetes. Hormone and Metabolic Research, 34, 150-154.
 Anitha, K., Gopi, G. and Kumar, P.S. (2013) Molecular Docking Study on Dipeotidyl Peptidase-4 Inhibitors. International Journal of Research and Development in Pharmacy and Life Sciences, 2, 602-610.
Wang, J.M., Hou, T.J. and Xu, X.J. (2006) Recent Advances in Free Energy Calcula-tions with a Combination of Molecular Mechanics and Continuum Models. Current Computer-Aided Drug Design, 2, 287-306.
Kollman, P.A., Massova, I., Reyes, C., et al. (2000) Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models. Accounts of Chemical Research, 33, 889-897.