Fluorescence study on the interaction of human serum albumin with loureirin BReport as inadecuate




Fluorescence study on the interaction of human serum albumin with loureirin B - Download this document for free, or read online. Document in PDF available to download.

Spectroscopy - Volume 24 2010, Issue 5, Pages 547-557



Experimental Center for Life Sciences, School of Life Sciences, Shanghai University, Shanghai, China

College of Sciences, Shanghai University, Shanghai, China

Department of Biomedical Engineering, University of Southern California, Los Angeles, USA

Experimental Center for Life Sciences, School of Life Sciences, Shanghai University, 99 Shang Da Road, Shanghai, 200444, China



Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The interaction between loureirin B Lour B and human serum albumin HSA was investigated by fluorescence and UV–vis absorption spectroscopy. Experimental results indicated that loureirin B had a strong ability to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The fluorescence quenching data revealed that the quenching constants KSV 2.68×10

, 3.30×10

and 4.10×10

l-mol at 300, 310 and 320 K, respectively. Based on the thermodynamic parameters obtained, the positive values of enthalpy change ΔH and entropy change ΔS suggested that hydrophobic forces played a major role in the interaction of Lour B with HSA. According to Förster theory of energy transfer, the distance r between HSA and Lour B was calculated to be 2.85 nm. Furthermore, the effect of Lour B on the conformation of HSA was analyzed by synchronous fluorescence and three-dimensional fluorescence spectra.





Author: Xu Chen, Jia-Ming Ma, Ke-Lan Yong, Jing-Ci Lv, and Xia-Bing Zhang

Source: https://www.hindawi.com/



DOWNLOAD PDF




Related documents