Infrared spectroscopy of human serum albumin in the presence of metal ions

Abstract

The interaction of human serum albumin (HSA) with divalent metal ions Ca2+ and Mn2+ was studied at various molar ratios [Me2+] : [HSA]. The interaction was studied by means of FTIR spectroscopy and protein heat denaturation in solution. Based on the analysis of the FTIR spectra we have shown that the interaction of HSA with Ca2+ and Mn2+ ions in solution leads to increase in the amount of β-sheet structures accompanied by decreasing α-helical content in the protein’s secondary structure. However, experiments of protein heat denaturation in solution has demonstrated that the mechanism of these changes is different for Ca2+ and Mn2+. Refs 15. Figs 4. Tables 2.