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Spectroscopic investigation of the interaction between rifabutin and bovine serum albumin

Paper ID Volume ID Publish Year Pages File Format Full-Text
27954 44052 2007 6 PDF Available
Title
Spectroscopic investigation of the interaction between rifabutin and bovine serum albumin
Abstract

The binding of rifabutin (RB) to bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and circular dichroism (CD). RB effectively quenched the intrinsic fluorescence of BSA via a combination of static and dynamic quenching. The thermodynamic parameters, ΔH° and ΔS° were estimated to be −5.14 kJ mol−1, +120.44 J mol−1 K−1 according to the van’t Hoff equation. This indicates that hydrophobic interaction plays a major role in stabilizing the RB–BSA complex. The high order of magnitude of kq (1015) for RB–BSA suggests that the process of energy transfer occurs through intermolecular interaction. Binding studies in the presence of fluorescence probe, 8-anilino-1-naphthalein-sulphonic acid (ANS), showed that RB competed with ANS for hydrophobic sites on the surface of BSA. The effect of metal ion on the binding constant of RB–BSA complex varied with metal ion. Cu2+ and Ca2+ increased the binding constant, whereas Zn2+ and Mg2+ decreased the binding efficacy of RB to BSA. Synchronous fluorescence spectra and CD data revealed that RB induced the conformational change of BSA.

Keywords
Rifabutin (RB); Bovine serum albumin (BSA); Fluorescence quenching; Synchronous fluorescence; Circular dichroism (CD)
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Spectroscopic investigation of the interaction between rifabutin and bovine serum albumin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 192, Issue 1, 15 November 2007, Pages 23–28
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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