Study of Binding Interactions of Human Carbonic Anhydrase Xii

Abstract

Objective: The present study was carried out to study the binding interactions of different N'-(substituted phenyl sulfonyl)-pyridine-2-carbohydrazide derivatives and N'-(substituted phenyl sulfonyl)-thiophene-2-carbohydrazide derivatives which were synthesized by senior students from research laboratory, with objective to explore the suitability of selected ligands for their binding affinity for the selected target.Methods: Binding interactions of the selected ligands were studied using glide module of Schrodinger software using Maestro 10.1 interface. At the end of molecular docking studies, docking scores along with 2D and 3D binding interactions of these ligands were studied to evaluate the potency of ligands to act as selective human carbonic anhydrase (hCAXII) inhibitors in comparison with standard inhibitor Acetazolamide (AZA).Results: Docking study on the ligands exhibited very similar conformation and binding interactions with hCAXII as that of standard. This suggests that selected ligands might possess significant binding affinity for hCAXII. Conclusion:It can be concluded that the selected ligands have the potential to act as inhibitors of hCAXII.

In Silico Molecular Modeling and Docking of Apigenin Against the Lung Cancer Cell Proteins

“…In this study, cellular tumor antigen p53, caspase 3, and mucosal addressin cell molecule 1 were successfully docked with apigenin using the BSP- Slim server. Based on the negative and lowest energy value (D G bind), the best docking orientation was chosen [30,31]. Docking analysis showed that there was a strong interaction between cellular tumor antigen p53 and apigenin.…”