Issue 23, 2005

Binding of a chiral drug to a protein: an investigation of the 2-(3-benzoylphenyl)propionic acid/bovine serum albumin system by circular dichroism and fluorescence

Abstract

A combined approach using global analysis of circular dichroism multiwavelength data and time resolved fluorescence was applied to investigate the interaction of R-(−)- and S-(+)-ketoprofen with bovine serum albumin in buffer solution at neutral pH. A characterization of the most stable drug : protein adducts of 1 : 1 and 2 : 1 stoichiometry, as individual chemical species, was obtained. The stability constants and the absolute circular dichroism spectra of the diastereomeric complexes were determined. The spectra of the 1 : 1 conjugates are opposite in sign, those of the 2 : 1 complexes are both negative, but different in shape from each other (peaks at 358 and 342 nm for S-(+)- and R-(−)-ketoprofen, respectively). A tryptophan residue was shown to be involved in the binding of the drug, in the primary site for the R-(−) and in the secondary site for the S-(+) enantiomer, thereby showing that chiral recognition by the protein causes the site of highest affinity being not the same for both optical antipodes.

Graphical abstract: Binding of a chiral drug to a protein: an investigation of the 2-(3-benzoylphenyl)propionic acid/bovine serum albumin system by circular dichroism and fluorescence

Article information

Article type
Paper
Submitted
12 Jul 2005
Accepted
20 Sep 2005
First published
04 Oct 2005

Phys. Chem. Chem. Phys., 2005,7, 4002-4008

Binding of a chiral drug to a protein: an investigation of the 2-(3-benzoylphenyl)propionic acid/bovine serum albumin system by circular dichroism and fluorescence

S. Monti, F. Manoli, S. Sortino, R. Morrone and G. Nicolosi, Phys. Chem. Chem. Phys., 2005, 7, 4002 DOI: 10.1039/B509911K

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