Studies on the interaction between chromium(VI) and human serum albumin: Spectroscopic approach
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- 作者：Gen-Cheng Zhanga ; b ; genchengzhang@126.com ; Jie-Yan Xua ; b ; Yan-Qing Wanga ; b ; wyqing76@126.com
- 关键词：Chromium(VI) ; Human serum albumin ; Fluorescence spectroscopy ; Binding parameters
- 刊名：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
- 出版年：2012
- 出版时间：February, 2012
- 年：2012
- 卷：86
- 期：Complete
- 页码：381-386
- 全文大小：1005 K
文摘
The interaction between Cr2O72?/sup> 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 Cr2O72?/sup> 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 Cr2O72?/sup> 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 Cr2O72?/sup> altered the environments of Trp and Tyr residues in HSA.