Impact of K2PtCl4 on the structure of human serum albumin and its binding ability of heme and bilirubin.

Absorption, CD, gel-filtration chromatography, and immunological tests were used to evaluate the interactions of K2PtCl4 with human serum albumin. Multidentate coordination of Pt(II) to HSA causes distinct variations in the protein conformation including a considerable decrease of the helical structure. The high excess of Pt(II) ions leads to dimerization of the protein. The metal ion binding weakness the interactions of HSA with other molecules like heme or bilirubin.