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Issue 29, 2013
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Probing deep into the interaction of a fluorescent chalcone derivative and bovine serum albumin (BSA): an experimental and computational study

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Abstract

In the present manuscript, a novel fluorescent chalcone derivative is synthesized and its photophysical properties are fully characterized. The designed fluorophore is applied as a probe to study protein–dye interactions with bovine serum albumin. Circular dichroism gave interesting results on the thermodynamics of the interaction. NMR spectroscopy, especially relaxation measurements, revealed the atoms in the chalcone derivative that interacts with the protein upon binding. Molecular docking calculations indicate that the most favourable binding sites are near the two tryptophan residues. Furthermore, ab initio and DFT calculations offer insights into the reactivity and physicochemical properties of this novel fluorophore.

Graphical abstract: Probing deep into the interaction of a fluorescent chalcone derivative and bovine serum albumin (BSA): an experimental and computational study

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Publication details

The article was received on 30 Nov 2012, accepted on 30 Apr 2013 and first published on 16 May 2013


Article type: Paper
DOI: 10.1039/C3OB27331H
Citation: Org. Biomol. Chem., 2013,11, 4764-4777
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    Probing deep into the interaction of a fluorescent chalcone derivative and bovine serum albumin (BSA): an experimental and computational study

    H. G. O. Alvim, E. L. Fagg, A. L. de Oliveira, H. C. B. de Oliveira, S. M. Freitas, M. E. Xavier, T. A. Soares, A. F. Gomes, F. C. Gozzo, W. A. Silva and B. A. D. Neto, Org. Biomol. Chem., 2013, 11, 4764
    DOI: 10.1039/C3OB27331H

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