Kassa, Solomon BezabehTaslimi, ParhamÖzel, ŞahinGür, BahriGülçin, İlhamiÖnganer, Yavuz2024-06-132024-06-132021-10-280927-7757https://doi.org/10.1016/j.colsurfa.2021.127839https://www.sciencedirect.com/science/article/pii/S0927775721017088https://hdl.handle.net/11452/42148This 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.eninfo:eu-repo/semantics/closedAccessBiological evaluationCarbonic-anhydraseMolecular dockingCrystal-structureGlucosidaseButyrylcholinesteraseAcetylcholinesteraseDegradationStabilityBiosensorAlpha-glycosidasePluronic (r) f127ImmobilizationEnzyme inhibitionPhenolic compounds, negative binding energyChemistryArticle00071866590000263210.1016/j.colsurfa.2021.1278391873-4359