Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
Volume 124, Issue -, Pages 50-62Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2013.04.004
Keywords
Carmoisine; Serum proteins; Fluorescence quenching; Specific binding; Thermodynamic parameters
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Funding
- DST-India [SR/FTP/CS-97/2006]
- CSIR-India [01/(2177)/07 EMR-II]
- IIT-Kharagpur (ISIRD-EEM)
- IIT Kharagpur
- CSIR-India
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Here we have investigated the binding of carmoisine, a water-soluble azo food colorant, with serum proteins (HSA and BSA) by fluorescence and UV-VIS spectroscopy, circular dichroism and molecular docking studies. Results indicate that fluorescence quenching of protein has been due to site-specific binding of the dye with biomacromolecules. Site marker competitive binding and molecular docking explorations show that interaction occurs in the sub-domain IIA of HSA and the sub-domains IIA and IB in the case of BSA. Conformational investigation indicates that dye binding modifies the secondary structure of proteins and this also alters the microenvironment of the tryptophan(s). The interaction is found to be pH-insensitive which can have relevance to the toxicological profiles of the dye, and ionic strength dependence of binding can be exploited in protein purification mediated by such food colorants. (C) 2013 Elsevier B.V. All rights reserved.
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