The HSA affinity of warfarin and flurbiprofen determined by fluorescence anisotropy measurements of camptothecin.

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Wybranowski T, Cyrankiewicz M, Ziomkowska B, Kruszewski S

The HSA affinity of warfarin and flurbiprofen determined by fluorescence anisotropy measurements of camptothecin.

Biosystems. 2008 Dec;94(3):258-62. doi: 10.1016/j.biosystems.2008.05.034. Epub 2008 Jul 31.

PubMed ID

18721856 [ View in PubMed

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Abstract

The determination of affinity of warfarin and flurbiprofen to human serum albumin (HSA) by fluorescence anisotropy measurements of carboxylate form of camptothecin (CPT-C) is the subject of this paper. A simple method based on measurements of fluorescence anisotropy of CPT-C allows to determine the affinity constant of CPT-C to HSA by computation of the fraction of bound CPT-C molecules with HSA It was observed, that adding of competing drug to plasma significant reduces the rate of increase of CPT-C fluorescence anisotropy with increase of albumin concentration and, the affinity constant of CPT-C to HSA decreases. The hypothesis of interactions between competing drug and CPT-C is presented. The results of these studies suggest that CPT-C displaces other drug from protein binding site and the degree of this displacement depends on concentration of drug and drug-HSA binding affinity. The presented in this paper biosystems research allows to estimate the affinity constant of warfarin and flurbiprofen. It was also confirmed that despite that most of drugs bind predominantly to Site I or Site II of HSA (only one of these sites is high-affinity site), at elevated concentrations, part of drug molecules can be bound to low-affinity site of HSA.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Warfarin	Serum albumin	Protein	Humans	No	Binder Regulator	Details