Biochanin obstructs human serum albumin from non-enzymatic glycation: an in vitro approach

Abstract

Various serum proteins, like Human Serum Albumin (HSA) and others, are susceptible to glycation and the formation of Advanced Glycation End Products (AGEs). Diabetes and other diseases are associated with AGE development. Recently, isoflavones have been studied for their therapeutic benefits. In the present study, we glycated HSA with Methylglyoxal (MGO) with and without the test compound, i.e., Biochanin A (BCA), to test its antiglycating capacity. We studied the biochemical and biophysical effects of glycation on HSA with and without BCA and also took the help of the in silico technique. Analytical methods included intrinsic and extrinsic fluorescence, polyacrylamide gel electrophoresis (PAGE), UV spectroscopy, far UV circular dichroism, and others. For structural comprehension, TEM and SEM were used. Molecular docking and simulation were employed to observe BCA-HSA's site-specific interaction. Since HSA is a therapeutically relevant protein involved in many disorders, this study’s findings are important.

Communicated by Ramaswamy H. Sarma

Keywords:

• Biochanin A
• human serum albumin
• methylglyoxal
• glycation

Acknowledgements

The authors express their gratitude for the opportunity to use the DST-FIST instruments facilities of the Department of Biochemistry, J.N. Medical College, Department of Biochemistry (Life Science Faculty), and the support from USIF, all of which are located within the boundaries of Aligarh Muslim University. The author also expresses her gratitude to the Council of Scientific and Industrial Research (CSIR), New Delhi for the Senior Research Scholarship. Authors also acknowledge the co-operation of her lab-mates and Mr. Rizwan Khan (Scholar, Department of Biochemistry, Life Science, AMU).

Disclosure statement

The authors declare there is no conflict of interest in this work.

Additional information

Funding

This research did not receive any specific grant from funding agencies in the public, commercial, or not-for-profit sectors.