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Characterization of the interaction between reserpine and bovine serum albumin: Spectroscopic approaches

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Title Characterization of the interaction between reserpine and bovine serum albumin: Spectroscopic approaches
 
Creator Wang, Tianhu
Zhao, Zhimin
Hua, Jin
Zhang, Jihua
 
Subject Reserpine
Bovine serum albumin
Fluorescence quenching
Fourier transformed infrared
Thermodynamic parameter
 
Description 388-394
The characteristics of the interaction between reserpine and bovine serum
albumin (BSA) were studied by fluorescence, UV-vis absorption and Fourier
transform infrared (FT-IR) spectroscopy. Spectroscopic analysis revealed that
fluorescence quenching of BSA by reserpine was through a static quenching
procedure. The binding constant KA
of reserpine with BSA at 293, 301 and 309 K was 1.63, 1.78 and 2.35 × 105
moL-1 L respectively, which indicated degree of binding force
between reserpine and BSA. There was one binding site between reserpine and
BSA. The entropy and enthalpy changes were positive, indicating that
interaction of reserpine and BSA was driven mainly by hydrophobic forces. The
average binding distance between the donor (BSA) and the acceptor (reserpine)
was about 3.84 nm based on the Förster non-radiation energy transfer theory.
Results of synchronous fluorescence and FT-IR spectra indicated that the
conformation and microenvironment of BSA were changed by the binding of
reserpine. The results may provide important insights into the physiological
activity of reserpine.
 
Date 2011-12-23T10:31:21Z
2011-12-23T10:31:21Z
2011-12
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/13253
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.48(6) [December 2011]