靶向DPP4与2型糖尿病相关药物分子的对接研究

The Docking of Protein DPP4 and Drug Molecules for Type 2 Diabetes

摘要: DPP-4抑制剂作为一种治疗2型糖尿病的新型药物正在崭露头角，本文利用分子对接技术研究DPP4蛋白与5种抑制剂之间的对接研究，以期对新的抑制剂的研究提供帮助。结果表明：阿格列汀抑制剂与DPP4对接过程中与GLU206，TYR662，ARG125处结合形成氢键，与GLU205处形成盐桥；沙格列汀与DPP4对接过程中在GLU205，GLU206、TYR662，ARG125部位形成氢键，并在骨架的GLU205处形成氢键；利拉利汀与DPP4对接过程中在GLU205，TYR662，ARG125部位形成氢键，在GLU206处形成盐桥，而在TUR547处形成了π-π作用；西他列汀与DPP4对接过程中在GLU205，TYR662部位形成氢键，在GLU206处形成盐桥，而在TYR666处形成了π-π作用；维格列汀与DPP4对接过程中在GLU205部位形成氢键，在GLU206处形成盐桥。

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.