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Propionic Acid Groups and Multiple Aromatic Rings Induce Binding of Ketoprofen and Naproxen to the Hydrophobic Core of Bovine Serum Albumin.
Tsurushima, Minori; Kurosawa, Yuya; Goto, Satoru.
Afiliación
  • Tsurushima M; Faculty of Pharmaceutical Sciences, Division of Colloid and Surface Science, Research Institute for Science and Technology, Tokyo University of Science, 2641 Yamasaki, Noda, Chiba 278-8510, Japan.
  • Kurosawa Y; Faculty of Pharmaceutical Sciences, Division of Colloid and Surface Science, Research Institute for Science and Technology, Tokyo University of Science, 2641 Yamasaki, Noda, Chiba 278-8510, Japan.
  • Goto S; Faculty of Pharmaceutical Sciences, Division of Colloid and Surface Science, Research Institute for Science and Technology, Tokyo University of Science, 2641 Yamasaki, Noda, Chiba 278-8510, Japan.
Mol Pharm ; 20(7): 3549-3558, 2023 07 03.
Article en En | MEDLINE | ID: mdl-37337436
ABSTRACT
Ketoprofen (KP), which causes photosensitivity by interacting with serum albumin (SA), and three drugs, ibuprofen (IBP), naproxen (NPX), and diazepam (DZP), which share the same binding site, were investigated for their interaction with bovine SA (BSA). For KP, DZP, and IBP, where drug-concentration-dependent quenching of BSA-intrinsic fluorescence was observed, a modified Stern-Volmer plot showed that dynamic quenching was dominant for KP and static quenching was dominant for DZP and IBP. However, this alone cannot be compared with NPX. Therefore, by performing singular value decomposition (SVD) fluorescence spectroscopy, we were able to find the behavior of the drug-concentration-dependent Langmuir-type principal component vectors. KSVD obtained by the Langmuir equation showed a high correlation with the static extinction constant V. Therefore, KSVD indicates the association constant of the drug with BSA and it was found that NPX and IBP had higher values than KP. Finally, in the analysis of the temperature factors of amino acid residues in each drug-binding region and Trp residues, KP and NPX significantly reduced these temperature factors whereas DZP and IBP hardly changed them. This result is consistent with the dynamic and static quenching dominance in the total quenching mechanism. Summarizing the results so far, it was shown that penetration into the hydrophobic core inside BSA can be achieved not only by one of the multiple aromatic rings and propionic acid groups but also by the joint effect of both. In this study, SVD enabled us to extract information on drug adsorption to BSA from fluorescence spectra. Furthermore, the application of SVD is expected to make it possible to perform fluorescence analysis for drug binding to proteins without being limited by the fluorescence properties of the drug.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Albúmina Sérica Bovina / Cetoprofeno Idioma: En Revista: Mol Pharm Asunto de la revista: BIOLOGIA MOLECULAR / FARMACIA / FARMACOLOGIA Año: 2023 Tipo del documento: Article País de afiliación: Japón

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Albúmina Sérica Bovina / Cetoprofeno Idioma: En Revista: Mol Pharm Asunto de la revista: BIOLOGIA MOLECULAR / FARMACIA / FARMACOLOGIA Año: 2023 Tipo del documento: Article País de afiliación: Japón
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