Propionic Acid Groups and Multiple Aromatic Rings Induce Binding of Ketoprofen and Naproxen to the Hydrophobic Core of Bovine Serum Albumin.
drug adsorption
fluorescence
hapten
serum albumin
singular value decomposition
Journal
Molecular pharmaceutics
ISSN: 1543-8392
Titre abrégé: Mol Pharm
Pays: United States
ID NLM: 101197791
Informations de publication
Date de publication:
03 07 2023
03 07 2023
Historique:
medline:
4
7
2023
pubmed:
20
6
2023
entrez:
20
6
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 37337436
doi: 10.1021/acs.molpharmaceut.3c00169
pmc: PMC10324393
doi:
Substances chimiques
Serum Albumin, Bovine
27432CM55Q
Naproxen
57Y76R9ATQ
Ketoprofen
90Y4QC304K
propionic acid
JHU490RVYR
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3549-3558Références
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