A Data on molecular docking of Sulfamoyl phenyl derivatives on diabetic targeted human DPP-4 enzyme

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.