Enzyme Inhibition and Antioxidant Potential of New Synthesized Sulfonamides; Synthesis, Single Crystal and Molecular Docking

Abstract This study describes the synthesis of four (1-4) new phenylalanine based sulfonamides from benzene sulfonyl chlorides. The progress of the reaction was monitored on TLC and after completion; the products were subjected to various analyses that indicated the synthesis of the targeted molecules. The structure of sulfonamide 1 was elucidated on the basis of Single Crystal X-Ray Diffraction technique. While other sulfonamides were characterized with FTIR spectroscopy. The sulfonamide (1-4) were subjected to Density Functional Theory for optimization of the structures and to calculate the bond angle and bond length of the crystalline molecule (1). The DFT and SCXRD results are in close agreement with each other. All compounds were subjected to radical scavenging and enzyme inhibition studies. The compound 1 exhibited moderate antioxidant activity (38.04 %). Enzyme inhibition potential was checked against three enzymes; trypsin, acetylcholine esterase and butyrylcholine esterase using in-vitro models. This study indicated that 2-(4-acetamidophenylsulfonamido)-3-phenylpropanoic acid (1) was found most active among all the synthetic molecules. It exhibited inhibition of 54.07%, 72.42and 57.18 % against AChE, BChE and trypsin respectively. Docking studies of the four sulfonamides were also done with Molecular Operating Environment, which depicted good docking scores. In-silico studies also suggested good enzyme inhibition potential of these understudied molecules.