Experimental and Computational Interaction Studies of (E)-N’-Benzylidene-5-Methyl-1H-Pyrazole-3-Carbohydrazide with ?-Glucosidase and ?-Amylase Enzymes: A Detailed Structural, Spectroscopic, and Biophysical Study

Abstract

Herein we report the synthesis, DFT calculations, and molecular docking studies of a pyrazole derivative, (E)-N'-benzylidene-5-methyl-1H-pyrazole-3-carbohydrazide (E-BMPC) as ?-glucosidase and ?-amylase inhibitor. Molecular structure of E-BMPC has been confirmed by single crystal X-ray diffraction (XRD), FTIR, 1H, and 13C NMR spectra. In addition, density functional theory (DFT) calculations on E-BMPC were carried out to obtain frontier molecular orbital energies and first-order static hyperpolarizability (ß). The ?-amylase and ?-glucosidase enzyme inhibitory of E-BMPC was also tested. E-BMPC displayed moderate inhibitory activity with IC50 values 310.57 ± 2.67 and 182.19 ± 3.20 against ?-glucosidase and ?-amylase enzymes, respectively. Molecular docking analysis provided the inhibition constant of E-BMPC molecule for ?-amylase enzyme as 33.60 µM. Both in vitro and in silico enzyme inhibition studies showed that E-BMPC molecule is a better inhibitor for ?-amylase than ?-glucosidase. The ß parameter for the molecule under investigation was also calculated as 4.2 × 10-30esu. © 2022 Taylor & Francis Group, LLC.