Omeprazole inhibits α-glucosidase activity and the formation of nonenzymatic glycation products: Activity and mechanism.
J Biosci Bioeng
; 133(2): 110-118, 2022 Feb.
Article
in En
| MEDLINE
| ID: mdl-34802943
ABSTRACT
In this study, the inhibitory effect and mechanism of omeprazole on α-glucosidase and nonenzymatic glycation were investigated in vitro by using multi-spectroscopic methods and molecular docking. Enzyme kinetic results showed that omeprazole inhibited α-glucosidase in a reversible and noncompetitive manner (IC50= 0.595 ± 0.003 mM). The results from fluorescence quenching and thermomechanical analyses signified that omeprazole reduced the fluorescence intensity of α-glucosidase by forming an omeprazole-α-glucosidase complex primarily driven by hydrogen bonds. Molecular docking further confirmed that hydrogen bonds and hydrophobic forces were the major driving forces for omeprazole binding to α-glucosidase. The nonenzymatic glycation assays revealed that omeprazole had a moderate inhibition against the formation of fructosamine, dicarbonyl compounds, and advanced glycation end products (AGEs). This study provides a new inhibitor of both α-glucosidase and nonenzymatic glycation and provides a practicable candidate for treating diabetes and its complications.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Alpha-Glucosidases
/
Glycoside Hydrolase Inhibitors
Language:
En
Journal:
J Biosci Bioeng
Journal subject:
ENGENHARIA BIOMEDICA
/
MICROBIOLOGIA
Year:
2022
Document type:
Article
Affiliation country:
China