In silicoscreening for inhibitory potentiality towards protein structure tyrosine phosphatase 1Bof sulfonylureas derivatives

Sulfonylureas derivatives were demonstrated to be effective inhibitors towards α‐glucosidase, thus also expected possessing inhibitory potentiality towards tyrosine phosphatase structure 1B. Five new sulfonylureas derivatives (S1‐S5), exhibiting α‐glucosidase inhibition activity, were selected for in silicoscreening for inhibitability towards UniProtKB‐PTP1B structure. Density functional theory confirms their existence; natural bond orbital analysis infers their stability; electronic transferability suggests their capability regarding intermolecular interaction. Docking‐based investigation interprets the inhibitory potentiality of the compounds into the order of complexes: S3‐PTP1B> S4‐PTP1B> S1‐PTP1B> S5‐PTP1B> S2‐PTP1B. QSARS‐based analysis specifies S4as the most physicochemically and pharmaceutically compatible candidate for the general application as a protein inhibitor (Molecular mass: 213.9 amu; Dispersion coefficient: LogP 4.01; DSaverage: 11.9 kcal.mol‐1). The computer‐based findings encourage further confirmation from experiment‐based researches and development for a versatile inhibitor towards diabetes‐related protein structures (aka. α‐glucosidase and tyrosine phosphatase structure 1B).