Characterization of the interaction between reserpine and bovine serum albumin: Spectroscopic approaches
IR@NISCAIR: CSIR-NISCAIR, New Delhi - ONLINE PERIODICALS REPOSITORY (NOPR)
View Archive Info| Field | Value | |
| Title |
Characterization of the interaction between reserpine and bovine serum albumin: Spectroscopic approaches
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| Creator |
Wang, Tianhu
Zhao, Zhimin Hua, Jin Zhang, Jihua |
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| Subject |
Reserpine
Bovine serum albumin Fluorescence quenching Fourier transformed infrared Thermodynamic parameter |
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| Description |
388-394
<span style="font-size:11.0pt;font-family: " times="" new="" roman","serif";mso-fareast-font-family:"times="" roman";mso-bidi-font-family:="" mangal;mso-ansi-language:en-gb;mso-fareast-language:en-us;mso-bidi-language:="" hi"="" lang="EN-GB">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 <i style="mso-bidi-font-style:normal">K</i><sub>A</sub> of reserpine with BSA at 293, 301 and 309 K was 1.63, 1.78 and 2.35 × 10<sup>5</sup> moL<sup>-1</sup> 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.</span> |
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| Date |
2011-12-23T10:31:21Z
2011-12-23T10:31:21Z 2011-12 |
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| Type |
Article
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| Identifier |
0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/13253 |
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| Language |
en_US
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| Rights |
<img src='http://nopr.niscair.res.in/image/cc-license-sml.png'> <a href='http://creativecommons.org/licenses/by-nc-nd/2.5/in' target='_blank'>CC Attribution-Noncommercial-No Derivative Works 2.5 India</a>
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| Publisher |
NISCAIR-CSIR, India
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| Source |
IJBB Vol.48(6) [December 2011]
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