Article 2022 · 20 citations

Effects of some phenolic compounds on the inhibition of α-glycosidase enzyme-immobilized on Pluronic®F127 micelles: An in vitro and <i>in</i> <i>silico</i> study

Kassa, Solomon Bezabeh, Taslimi, Parham, Ozel, Sahin, Gur, Bahri, Gulcin, Ilhami, Onganer, Yavuz

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.

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

WoS Categories

Chemistry, Physical

Sustainable Development Goals

Good Health and Well-being

Citation

Journal: COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
Year: 2022
Volume: 632
ISSN: 0927-7757
eISSN: 1873-4359
DOI: 10.1016/j.colsurfa.2021.127839
WoS UID: WOS:000718665900002

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