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Your search keyword '"Drug/protein binding"' showing total 2 results
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2 results on '"Drug/protein binding"'

1. Ultrafast Fluorescence Dynamics in Flurbiprofen–Amino Acid Dyads and in the Supramolecular Drug/Protein Complex

Author

Ignacio Vayá, M. Consuelo Jiménez, Miguel A. Miranda, Aninda Chatterjee, and Thomas Gustavsson

Subjects
Drug/protein binding, Fluorescence upconversion, Flurbiprofen, Human serum albumin, Time-correlated single photon counting, Time-resolved fluorescence, Chemistry, QD1-999
Abstract

The interaction dynamics between the drug flurbiprofen (FBP) and human serum albumin (HSA) has been investigated by time-resolved fluorescence spectroscopy, combining femtosecond fluorescence upconversion and picosecond time-correlated single photon counting. In order to obtain additional information on the drug/ protein interaction, several covalently linked model dyads, composed of FBP and tryptophan or tyrosine, were also studied. For all systems, the main feature was a remarkable dynamic FBP fluorescence quenching, more prominent in the dyads than in the protein complex. All systems also displayed a clear stereoselectivity depending on the (S)- or (R)-form of FBP, that was strongly influenced by the conformational arrangement of the investigated chromophores.

Published
2017
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2. Ultrafast Fluorescence Dynamics in Flurbiprofen–Amino Acid Dyads and in the Supramolecular Drug/Protein Complex

Author

Thomas Gustavsson, Ignacio Vayá, Jiménez Mc, Aninda Chatterjee, Miguel A. Miranda, Departamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos (DEPARTAMENTO DE BIOTECNOLOGíA), CSIC, Espagne, Laboratoire Interactions, Dynamiques et Lasers (ex SPAM) (LIDyl), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Dynamique et Interactions en phase Condensée (DICO), Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Laboratoire Interactions, Dynamiques et Lasers (ex SPAM) (LIDyl), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Biomolécules Excitées (DICO), and Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Time Factors, Macromolecular Substances, Supramolecular chemistry, Time-correlated single photon counting, Plasma protein binding, 010402 general chemistry, Photochemistry, 01 natural sciences, Fluorescence, Fluorescence spectroscopy, TYROSINE, 0103 physical sciences, medicine, Humans, Amino Acids, QD1-999, Serum Albumin, Molecular Structure, 010304 chemical physics, Chemistry, Tryptophan, Human serum albumin, Time-resolved fluorescence, General Medicine, General Chemistry, Chromophore, Drug/protein binding, 3. Good health, 0104 chemical sciences, TRYPTOPHAN, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Flurbiprofen, Tyrosine, Time-resolved spectroscopy, Fluorescence upconversion, medicine.drug
Abstract

The interaction dynamics between the drug flurbiprofen (FBP) and human serum albumin (HSA) has been investigated by time-resolved fluorescence spectroscopy, combining femtosecond fluorescence upconversion and picosecond time-correlated single photon counting. In order to obtain additional information on the drug/ protein interaction, several covalently linked model dyads, composed of FBP and tryptophan or tyrosine, were also studied. For all systems, the main feature was a remarkable dynamic FBP fluorescence quenching, more prominent in the dyads than in the protein complex. All systems also displayed a clear stereoselectivity depending on the (S)- or (R)-form of FBP, that was strongly influenced by the conformational arrangement of the investigated chromophores.

Published
2017
Full Text
View/download PDF

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