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 (Articolo in rivista)

Type
Label
  • 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 (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1039/b509911k (literal)
Alternative label
  • Monti S., Manoli F., Sortino S., Morrone R., Nicolosi G. (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
    in PCCP. Physical chemistry chemical physics (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Monti S., Manoli F., Sortino S., Morrone R., Nicolosi G. (literal)
Pagina inizio
  • 4002 (literal)
Pagina fine
  • 4008 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://pubs.rsc.org/en/Content/ArticleLanding/2005/CP/b509911k (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 7 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto per la Sintesi Organica e la Fotoreattivita`-ISOF, CNR CNR Area della Ricerca, Bologna Dipartimento di Scienze Chimiche, Universita` di Catania Istituto di Chimica Biomolecolare-Sezione di Catania (literal)
Titolo
  • 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 (literal)
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-(þ)-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-(þ)- 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-(þ) enantiomer, thereby showing that chiral recognition by the protein causes the site of highest affinity being not the same for both optical antipodes. (literal)
Prodotto di
Autore CNR

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it