磷酸西他列汀
对接(动物)
磷酸西他列汀
氢键
生物信息学
二肽基肽酶-4
化学
生物化学
立体化学
医学
内分泌学
2型糖尿病
有机化学
分子
基因
护理部
糖尿病
2型糖尿病
作者
Michelangelo Bauwelz Gonzatti,José Telmo Valença Júnior,Anderson Rocha,Jonathas Sales de Oliveira,Antônio José de Jesus Evangelista,Fátima Morgana Pio Fonseca,Vânia Marilande Ceccatto,Ariclécio Cunha de Oliveira,José Ednésio da Cruz Freire
标识
DOI:10.1016/j.advms.2023.10.002
摘要
Dipeptidyl peptidase 4 (DPP4) inactivates a range of bioactive peptides. The cleavage of insulinotropic peptides and glucagon-like peptide 1 (GLP1) by DPP4 directly influences glucose homeostasis. This study aimed to describe the mode of interaction between sitagliptin (an antidiabetic drug) and human DPP4 using in silico approaches. Docking studies were conducted using AutoDock Vina, 2D and 3D schematic drawings were obtained using PoseView and PLIP servers, and the DPP4-sitagliptin complex was visualized with Pymol software. The best affinity energy to form the DPP4-sitagliptin complex was E-value = - 8.1 kcal mol−1, as indicated by docking simulations. This result suggests a strong interaction. According to our observations, hydrophobic interactions involving the amino acids residues Tyr663 and Val712, hydrogen bonds (Glu203, Glu204, Tyr663, and Tyr667), π-Stacking interactions (Phe355 and Tyr667), and halogenic bonds (Arg123, Glu204, and Arg356) were prevalent in the DPP4-sitagliptin complex. Root Mean Square Deviation prediction also demonstrated that the global structure of the human DPP4 did not have a significant change in its topology, even after the formation of the DPP4-sitagliptin complex. The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.
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