New chalcone derivative, ethyl 2-(4-(3-(benzo[b]thiophen-2-yl)acryloyl)phenoxy)acetate: synthesis, characterization, DFT study, enzyme inhibition activities and docking study

Çelik F., Süleymanoğlu N., Ustabaş R., Türkan F., Güler H. İ. , Ünver Y. , ...More

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 2021 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Publication Date: 2021
  • Doi Number: 10.1080/07391102.2021.1969287
  • Keywords: Chalcone, DFT, cholinesterases, glutathione S-transferase, inhibition, molecular docking study, BIOLOGICAL EVALUATION, HARDNESS, NMR


Chalcone derivative, ethyl 2-(4-(3-(benzo[b]thiophen-2yl)acryloyl)phenoxy)acetate (I), was synthesized. Compound I was characterized by proton and carbon-13 nuclear magnetic resonance (H-1- and C-13- NMR), fourier transform infrared (FTIR) and mass (LC-ESI-MS/MS) spectroscopic methods. Density Functional Theory (DFT) calculations for compound I were performed at B3LYP/6-311++G(d,p) level. Optimized geometry, frontier molecular orbitals (HOMO; highest occupied molecular orbital; LUMO: lowest unoccupied molecular orbital), IR and NMR parameters of compound I were obtained. The evaluations reveal that the calculation results support the experimental results. The inhibition effects of compound I on cholinesterases and GST enzyme were investigated. K-i and inhibition concentration (IC50) values were calculated separately. Ki values of compound I were found for GST 14.19 +/- 2.15, for AChE 11.13 +/- 1.22 and for BChE 8.74 +/- 0.76 recpectively. The docking analysis of compound I supported the enzym inhibition activity exhibiting high inhibition constant and binding energy for three receptors. Compound I is strongly bound to AChE, huBChE and Glutathione S-transferase with binding energies -11.24, -8.56 and -10.39 kcal/mol, respectively. Communicated by Ramaswamy H. Sarma