Effects of some phenolic compounds on the inhibition of alpha-glycosidase enzyme-immobilized on Pluronic (R) F127 micelles: An in vitro and in silico study


Kassa S. B. , Taslimi P., ÖZEL Ş. , GÜR B., GÜLÇİN İ., ONGANER Y.

COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS, vol.632, 2022 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 632
  • Publication Date: 2022
  • Doi Number: 10.1016/j.colsurfa.2021.127839
  • Title of Journal : COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
  • Keywords: alpha-glycosidase, Pluronic (R) F127, Immobilization, Enzyme inhibition, Phenolic compounds, Negative binding energy, BIOLOGICAL EVALUATION, CARBONIC-ANHYDRASE, MOLECULAR DOCKING, CRYSTAL-STRUCTURE, GLUCOSIDASE, BUTYRYLCHOLINESTERASE, ACETYLCHOLINESTERASE, DEGRADATION, STABILITY, BIOSENSOR

Abstract

This study aimed to consider the activity of immobilized alpha-glycosidase, significant enzyme defined in serum glucose adjustment, on Pluronic (R) F127 micelles and to compare the results with theoretical molecular docking studies. The phenolic molecules were used for the activity studies, which play a crucial role in the inhibition of alpha-glycosidase by providing conservation against pathogen factors. The immobilization of alpha-glycosidase on Pluronic (R) F127 micelles showed higher kinetic activity towards p-nitrophenyl-D-glucopyranoside (pNPG) than the free one. The inhibition profiles from some phenolic molecules were observed impressively with IC50 values between 20.47 and 1118.68 nM and K-i values between 18.51 and 1087.53 nM against immobilized alpha-glycosidase. In addition, the inhibition effects of the studied phenolic compounds have been tested with calculated negative binding energies from theoretical molecular docking studies. Negative binding energy values were as - 6.1 and - 8.3 kcalmol(-1) for p-coumaric acid and tetrakis compounds, respectively.