Inhibition on α-glucosidase activity and non-enzymatic glycation by an anti-oxidative proteoglycan from Ganoderma lucidum. - GreenMedInfo Summary
Inhibition onα-Glucosidase Activity and Non-Enzymatic Glycation by an Anti-Oxidative Proteoglycan from.
Molecules. 2022 Feb 22 ;27(5). Epub 2022 Feb 22. PMID: 35268560
Ying Zhang
The prevention of postprandial hyperglycemia and diabetic complications is crucial for diabetes management. Inhibition ofα-glucosidase to slow carbohydrate metabolism is a strategy to alleviate postprandial hyperglycemia. In addition, suppression of non-enzymatic glycation can diminish the advanced glycation end products and reduce the oxidative stress and inflammation, thereby preventing the diabetic complications.In this study, an anti-oxidative proteoglycan (named) extracted fromwas investigated in vitro for its inhibitory effect onα-glucosidase and non-enzymatic glycation using molecular kinetics, intrinsic fluorescence assay, and bovine serum albumin glycation models. The molecular kinetics and fluorescence assay revealed thatdecreasesα-glucosidase activity by forming a-α-glucosidase complex. To evaluate the anti-glycation effect, fructose-glycated and methylglyoxal-glycated BSA models were analyzed by spectroscopic and SDS-PAGE methods. Results showed thatinhibited the glycation at every stage and suppressed glycoxidation, possibly due to its anti-oxidative capacity and-BSA complex formation. Furthermore, we demonstrated in vivo thatcould alleviate postprandial hyperglycemia inmice as well as AGE accumulation and vascular injury in diabetic rats. Overall,possesses anti-postprandial hyperglycemia and anti-glycation functions and would be potentially used in clinic for diabetes and related complication management.