In this work, the method of FTIR spectroscopy on the ATR crystal with deconvolution of the Amide I band was used to study the secondary structure of the protein. The tertiary structure of HSA was studied by detection of absorption
and intrinsic fluorescence spectra of the protein. The zeta potential method was used to characterize the surface charge of protein particles. In this study, we investigated the HSA in the solution of metal ions Mg2+, Mn2+, Co2+ and Cu2+
when the concentration of metal ions was varied in the range of [Co2+]:[HSA] from 0 to 100, [Mg2+]:[HSA] from 0 to 10000, [Mn2+]:[HSA] from 0 to 50, [Cu2+]:[HSA] from 0 to 50.