Abstrait

Non-Enzymatic Glycation with D-Glucose Impairs the Biological Function of Human Serum Albumin: Relevance in Diabetes Mellitus

Alok Raghav

Human serum albumin (HSA) non-enzymatic glycation leads to the development of advanced glycation end products (AGEs). HSA was modified with D-glucose for a time span of 40 days at 370C. Post formation of AGEs, the native and glycated-HSA were evaluated for metformin hydrochloride, Cu (II) and oleic acid binding using spectroscopic techniques including UV, fluorescence, and FTIR. The molecular docking with fatty acids and HSA was also performed both in the presence and absence of glucose. The results showed functional impairments of HSA upon non-enzymatic glycation with glucose. The results of the present study clearly showed that hyperglycemia in diabetes mellitus leads to impairments in transport and binding property of HSA.