In silico screening for inhibitory potentiality towards protein structure tyrosine phosphatase 1B of sulfonylureas derivatives

Sulfonylureas derivatives were demonstrated to be effective inhibitors towards alpha-glucosidase, thus also expected possessing inhibitory potentiality towards tyrosine phosphatase structure 1B. Five new sulfonylureas derivatives (S1-S5), exhibiting alpha-glucosidase inhibition activity, were selected for in silico screening 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 S4 as 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. alpha-glucosidase and tyrosine phosphatase structure 1B).