Interaction between warfarin and bovine serum albumin detected by spectrometry.
- Author:
Yang YAN
1
;
Ruo-hui PEI
;
Hong-tao YAN
Author Information
1. First Affiliated Hosptical, Medical School of Xi' an Jiaotong University, Xi' an 710061, China.
- Publication Type:Journal Article
- MeSH:
Energy Transfer;
Protein Binding;
Serum Albumin, Bovine;
chemistry;
Spectrometry, Fluorescence;
methods;
Spectrophotometry, Ultraviolet;
methods;
Thermodynamics;
Warfarin;
chemistry
- From:
Acta Pharmaceutica Sinica
2008;43(12):1224-1227
- CountryChina
- Language:Chinese
-
Abstract:
The interaction between warfarin and bovine serum albumin (BSA) under pseudophysiological conditions was investigated by UV-Vis absorption spectrometry and spectrofluorimetry. The quenching mechanism of BSA by warfarin was discussed. It showed that the quenching process was a dynamic quenching, and the quenching constants were 6.05 x 10(4) L x mol(-1) at 16 degrees C and 6. 14 x 10(4) L x mol(-1) at 37 degrees C, separately. Based on the Förster theory of non-radiative energy transfer, the energy transfer efficiency and the distance of BSA to warfarin were calculated, which was 0.37 and 3.15 nm, respectively.
