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24 results on '"Ariese, Freek"'

2. Label‐free stimulated Raman scattering imaging reveals silicone breast implant material in tissue

Author

Haasterecht, Ludo, primary, Zada, Liron, additional, Schmidt, Robert W., additional, Bakker, Erik, additional, Barbé, Ellis, additional, Leslie, Heather A., additional, Vethaak, A. Dick, additional, Gibbs, Susan, additional, Boer, Johannes F., additional, Niessen, Frank B., additional, Zuijlen, Paul P. M., additional, Groot, Marie Louise, additional, and Ariese, Freek, additional

Published
2020
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9. Stereoselective binding of flurbiprofen enantiomers and their methyl esters to human serum albumin studied by time-resolved phosphoresce

Author

Lammers, Ivonne, Lhiaubet, Virginie Lyria, Jiménez Molero, María Consuelo, Ariese, Freek, Miranda Alonso, Miguel Ángel, and Gooijer, Cees

Subjects
nonlinear Stern-Volmer plot, QUIMICA ORGANICA, Sudlow's binding sites, heavy atom effect, Dexter resonance energy transfer
Abstract

The interaction of the nonsteroidal anti-inflammatory drug flurbiprofen (FBP) with human serum albumin (HSA) hardly influences the fluorescence of the protein's single tryptophan (Trp). Therefore, in addition to fluorescence, heavy atom-induced room-temperature phosphorescence is used to study the stereoselective binding of FBP enantiomers and their methyl esters to HSA. Maximal HSA phosphorescence intensities were obtained at a KI concentration of 0.2?M. The quenching of the Trp phosphorescence by FBP is mainly dynamic and based on Dexter energy transfer. The SternVolmer plots based on the phosphorescence lifetimes indicate that (R)-FBP causes a stronger Trp quenching than (S)-FBP. For the methyl esters of FBP, the opposite is observed: (S)-(FBPMe) quenches more than (R)-FBPMe. The SternVolmer plots of (R)-FBP and (R)-FBPMe are similar although their high-affinity binding sites are different. The methylation of (S)-FBP causes a large change in its effect on the HSA phosphorescence lifetime. Furthermore, the quenching constants of 3.0?x?107?M-1?s-1 of the R-enantiomers and 2.5?x?107?M-1?s-1 for the S-enantiomers are not influenced by the methylation and indicate a stereoselectivity in the accessibility of the HSA Trp to these drugs. Chirality 24:840846, 2012. (c) 2012 Wiley Periodicals, Inc., This research was financed by the Netherlands Organisation for Scientific Research NWO-CW (contract number ECHO 700.55.014) and by the Spanish Government MINECO (project CTQ2010-14882). VLV's stay at LaserLaB Amsterdam was supported by the EU Laserlab Europe program (contract number 2008-1-228334; project lcvu001484).

Published
2012

12. Stereoselective binding of flurbiprofen enantiomers and their methyl esters to human serum albumin studied by time-resolved phosphoresce

Author

Universitat Politècnica de València. Instituto Universitario Mixto de Tecnología Química - Institut Universitari Mixt de Tecnologia Química, Universitat Politècnica de València. Departamento de Química - Departament de Química, Ministerio de Ciencia e Innovación, Netherlands Organization for Scientific Research, European Commission, Lammers, Ivonne, Lhiaubet, Virginie Lyria, Jiménez Molero, María Consuelo, Ariese, Freek, Miranda Alonso, Miguel Ángel, Gooijer, Cees, Universitat Politècnica de València. Instituto Universitario Mixto de Tecnología Química - Institut Universitari Mixt de Tecnologia Química, Universitat Politècnica de València. Departamento de Química - Departament de Química, Ministerio de Ciencia e Innovación, Netherlands Organization for Scientific Research, European Commission, Lammers, Ivonne, Lhiaubet, Virginie Lyria, Jiménez Molero, María Consuelo, Ariese, Freek, Miranda Alonso, Miguel Ángel, and Gooijer, Cees

Abstract

The interaction of the nonsteroidal anti-inflammatory drug flurbiprofen (FBP) with human serum albumin (HSA) hardly influences the fluorescence of the protein's single tryptophan (Trp). Therefore, in addition to fluorescence, heavy atom-induced room-temperature phosphorescence is used to study the stereoselective binding of FBP enantiomers and their methyl esters to HSA. Maximal HSA phosphorescence intensities were obtained at a KI concentration of 0.2?M. The quenching of the Trp phosphorescence by FBP is mainly dynamic and based on Dexter energy transfer. The SternVolmer plots based on the phosphorescence lifetimes indicate that (R)-FBP causes a stronger Trp quenching than (S)-FBP. For the methyl esters of FBP, the opposite is observed: (S)-(FBPMe) quenches more than (R)-FBPMe. The SternVolmer plots of (R)-FBP and (R)-FBPMe are similar although their high-affinity binding sites are different. The methylation of (S)-FBP causes a large change in its effect on the HSA phosphorescence lifetime. Furthermore, the quenching constants of 3.0?x?107?M-1?s-1 of the R-enantiomers and 2.5?x?107?M-1?s-1 for the S-enantiomers are not influenced by the methylation and indicate a stereoselectivity in the accessibility of the HSA Trp to these drugs. Chirality 24:840846, 2012. (c) 2012 Wiley Periodicals, Inc.

Published
2012

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