Paper Title:
Spectroscopic Studies on the Interaction between Salvianolic Acid a and Human Serum Albumin
  Abstract

The interaction between human serum albumin (HSA) and salvianolic acid A (SA-A) was investigated by means of spectroscopy. The thermodynamic parameters ΔH and ΔS, had been calculated to be 148.94KJ·mol-1 > 0, and 640.85 J·mol-1·K-1 > 0, respectively. The distance between the donor (HSA) and receptor (SA-A), r, was obtained to be 2.49nm according to Förster's non-radiative energy transfer theory. The experimental results revealed that SA-A could quench the fluorescence of HSA by a static quenching mechanism. Furthermore, the binding constants between HSA and SA-A were obviously affected by metal ions, decreased in the presence of Co(Ⅱ) and Mg(Ⅱ), increased with Ni(Ⅱ) and Zn(Ⅱ), and no change with Cu(Ⅱ). The interaction between SA-A and HSA was driven mainly by hydrophobic force.

  Info
Periodical
Advanced Materials Research (Volumes 236-238)
Edited by
Zhong Cao, Yinghe He, Lixian Sun and Xueqiang Cao
Pages
2399-2402
DOI
10.4028/www.scientific.net/AMR.236-238.2399
Citation
T. Zhang, Q. W. Liu, G. H. Li, "Spectroscopic Studies on the Interaction between Salvianolic Acid a and Human Serum Albumin", Advanced Materials Research, Vols. 236-238, pp. 2399-2402, 2011
Online since
May 2011
Export
Price
$32.00
Share

In order to see related information, you need to Login.

In order to see related information, you need to Login.

Authors: Feng Yu Deng, Ying Liu
Chapter 1: Environmental Chemistry and Biology
Abstract:The effect of Fe3+ on the interaction between nitrofurazone (NF) and human serum albumin (HSA) was studied by fluorescence spectroscopy and...
337
Authors: Yu Fen Liu, Hai Tao Xia, De Fu Rong
Chapter 10: Chemical Biology and Medicinal Chemistry
Abstract:The binding reaction of Zn(II) complex [Zn(C8H10N)2Cl2] with bovine serum albumin(BSA) was...
1678