Studies on the interaction between chromium(VI) and human serum albumin: Spectroscopic approach

Abstract

The interaction between Cr 2O 7 2− and human serum albumin (HSA) was investigated using fluorescence, UV/vis, FT-IR, CD spectroscopy, and molecular modeling method. The experimental results showed that the fluorescence quenching of HSA by Cr 2O 7 2− is a result of the formation of HSA–chromium(VI) complex; static quenching was confirmed to result in the fluorescence quenching. The corresponding thermodynamic parameters showed that the process of binding Cr 2O 7 2− on HSA was a spontaneous molecular interaction procedure. Ionic, H-bonds and van der Waals interactions play a major role in stabilizing the complex. The Cr 2O 7 2− altered the environments of Trp and Tyr residues in HSA.