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Sci. Pharm. 2010, 78(4), 869-880; doi:10.3797/scipharm.1008-15

Interaction of Bioactive Coomassie Brilliant Blue G with Protein: Insights from Spectroscopic Methods

Department of Chemistry, Karnatak University, Dharwad 580 003, India
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Received: 26 August 2010 / Accepted: 6 November 2010 / Published: 6 November 2010
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Abstract

The binding of coomassie brilliant blue G (CBB) to bovine serum albumin (BSA) was investigated under simulative physiological conditions employing different optical spectroscopic techniques viz., fluorescence emission, UV–visible absorption and FTIR. Fluorescence quenching data obtained at different temperatures suggested the presence of dynamic type of quenching mechanism. The binding constant of CBB-BSA and the number of binding sites (n) for CBB in BSA were calculated and found to be 4.20 x 104 M−1 and 0.96 respectively, at 302 K. The value of n close to unity indicated that the protein has a single class of binding sites for CBB. The thermodynamic parameters revealed that the hydrophobic forces played a major role in the interaction of CBB to BSA. The distance between the CBB and protein was calculated using the theory of Föster’s Resonance Energy Transfer (FRET). The conformational change in the secondary structure of BSA upon interaction with dye was investigated by synchronous fluorescence and FTIR techniques. Competitive binding studies were also carried out to know the location of binding of CBB on BSA.
Keywords: Coomassie brilliant blue G; Physiological condition; Optical spectroscopy; Binding parameter; Thermodynamic parameter Coomassie brilliant blue G; Physiological condition; Optical spectroscopy; Binding parameter; Thermodynamic parameter
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

KATRAHALLI, U.; KALANUR, S.S.; SEETHARAMAPPA, J. Interaction of Bioactive Coomassie Brilliant Blue G with Protein: Insights from Spectroscopic Methods. Sci. Pharm. 2010, 78, 869-880.

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