Effect of magnesium(ii) on the glycation-induced oxidative stress of human serum albumin: a spectroscopic investigation

Abstract

Advanced glycation end (AGE) products lead to the generation of oxidative stress, which further leads to the development and progression of diabetic complications. In this current in vitro study, we focused on the interaction of magnesium(II) with glycated human serum albumin samples. Studies revealed that glycation leads to a reduction in the helical content of human serum albumin (HSA) and a rise in β-sheet content, denoting significant structural changes. In the presence of a physiological concentration of magnesium(II), however, the extent of the above reduction was significantly lower, leading to the preservation of the structural integrity of HSA. Partial reversibility in structure was, however, noted for native and glycated samples in temperature-dependent studies after the heating & cooling cycle. Observations in the UV & PL spectra of the various samples also demonstrated the same in the changing absorbance values of the various samples, while insights from the FTIR spectra revealed the changes occurring in the various bands and the fingerprint region of sugar. Lastly, the Raman shifts in the various bonds and amino groups, along with changes in the amide III region, were tracked. All the above observations show that Mg(II) can be potent in reducing AGE formation.