Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/13253
Title: Characterization of the interaction between reserpine and bovine serum albumin: Spectroscopic approaches
Authors: Wang, Tianhu
Zhao, Zhimin
Hua, Jin
Zhang, Jihua
Keywords: Reserpine;Bovine serum albumin;Fluorescence quenching;Fourier transformed infrared;Thermodynamic parameter
Issue Date: Dec-2011
Publisher: NISCAIR-CSIR, India
Abstract: 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.
Page(s): 388-394
URI: http://hdl.handle.net/123456789/13253
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.48(6) [December 2011]

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