A Data on molecular docking of Sulfamoyl phenyl derivatives on diabetic targeted human DPP-4 enzyme
Description
Type 2 diabetes mellitus endures a significant worldwide health burden, requiring effective and innovative treatment strategies. Dipeptidyl peptidase-4 (DPP-4) inhibitors have gained importance as therapeutic agents because they improve blood glucose control by stabilizing incretin hormones. The present study employs molecular docking simulations to evaluate the binding interactions between DPP-4 (PDB ID: 2OQV) and a series of synthesized 4-N-acetylsulfamoylphenyl, 4-N-pyrimidin-2-ylsulfamoyl phenyl, 4-N-5-methylisoxazol-4-yl sulfamoyl phenyl and N-4-sulfamoylphenyl derivatives. Docking analysis demonstrated favourable binding affinities, with scores ranging from -7.0 to -9.0 kcal/mol. Among the evaluated compounds, derivatives SULF24 exhibited the highest binding affinity (-9.0 kcal/mol), forming stable interactions with critical active site residues, including PRO:510, THR:565, VAL:558, LYS:512, ARG:560, ILE:529, thereby suggesting strong inhibitory potential. The remaining derivatives also displayed consistent interaction patterns within the enzymes binding pocket, further supporting their potential biological relevance. The observed molecular interactions and docking energetics underscore the potential of these sulfamoyl derivatives as promising lead molecule for further essay studies to optimized and validated these compounds, the development of advanced antidiabetic drugs.
Files
Steps to reproduce
• The data may be useful for researchers working on designing and exploration of new compounds development for diabetic management. • The data provide the potential and active molecules from synthetic procedure for further elemental analysis. • The data are important for synthesizing novel compounds of sulfamoylphenyl derivatives with DPP-4 inhibitors property.
Institutions
- Sharda UniversityUttar Pradesh, Greater Noida