Interaction of tetra-mu-acetatodirhodium(II) with human serum albumin

The interaction of Rh2(OAc)4 with human serum albumin (HSA) has been studied by absorption difference spectroscopy, CD spectroscopy, and quantitative precipitating HSA-antibody test. Our results demonstrate that this rhodium complex reacts easily with HSA at several ratios of reagents. The Rh atoms are coordinated to protein molecules via the imidazole rings of His residues. The structural studies have shown the conformational change of HSA modified by rhodium. Rhodium binding lowers the helicity of the native protein between 8 to 18% depending upon the molar ratios (from 1:1 to 10:1). Denaturation measurements of free HSA and HSA in the presence of dirhodium(II) acetate complex with 8-M urea followed by CD spectroscopy, suggest that rhodium affects the secondary protein structure and might stabilize HSA against denaturing agents. 8-M urea caused the unfolding of the native HSA secondary structure by about 40% and the structure of Rh(OAc)4-HSA by about 10%. The modification of native HSA by rhodium causes its decreased ability to precipitate with HSA antibodies. The decrease of antigenic properties can be connected with the unfolding of the antigen structure, which brings about perturbation of complementarity of the antigen-antibody reactive sites.