Structural changes of human serum albumin induced by cadmium acetate.

Abstract

The structural changes of human serum albumin (HSA) induced by the addition of cadmium acetate were systematically investigated using UV-vis absorption, circular dichroism (CD), synchronous, and three-dimentional (3D) fluorescence methods. The fluorescence spectra suggested the formation of cadmium acetate-HSA complex. UV absorption result indicated that the interaction between cadmium acetate and HSA could lead to the alteration of the protein skeleton. The structural analysis according to CD method showed that the cadmium acetate binding altered HSA conformation with a major reduction of α-helix, inducing a partial protein unfolding. Synchronous fluorescence spectra suggested that cadmium acetate was situated closer to tryptophan residue compared to tyrosine residues, making tryptophan residue locate in a more hydrophobic environment. 3D fluorescence demonstrated that cadmium acetate could induce the HSA aggregation and cause a slight unfolding of the polypeptide backbone of the protein.