Abstract
Hyperglycaemia accelerates the aging process significantly. Diabetes problems can be mitigated by inhibiting glycation. To learn more about glycation and antiglycation mediated by methyl glyoxal and baicalein, we studied human serum albumin as a model protein. A Methylglyoxal (MGO) incubation period of seven days at 37 degrees Celsius induced glycation of Human Serum Albumin.s Hyperchromicity, decreased tryptophan and intrinsic fluorescence, increased AGE-specific fluorescence, and reduced mobility were all seen in glycated human serum albumin (MGO-HSA) in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Fourier transform infrared spectroscopy (FT-IR) and then far ultraviolet dichroism were used to detect secondary and tertiary structural perturbations (CD). The Congo red assay (CR), scanning electron microscopy (SEM), and transmission electron microscopy (TEM) all verified the presence of amyloid-like clumps. Structure (carbonyl groups on ketoamine moieties) (CO), physiological problems including diabetes mellitus, and cardiovascular disease, etc. are linked to the structural and functional changes in glycated HSA, as proven by these studies.
Communicated by Ramaswamy H. Sarma
Acknowledgements
The authors gratefully acknowledge access to the DST-FIST instruments facilities of the Department of Biochemistry, J.N. Medical College and the support from USIF; all located within the premises of Aligarh Muslim. Authors are thankful to the University Grants Commission, New Delhi for Senior research fellowship.
Disclosure statement
Authors declare that there are no conflicts of interest.
Correction Statement
This article has been corrected with minor changes. These changes do not impact the academic content of the article.