Binding Sites of Fluorescent Probes on Human Serum Albumin

Muller, Noëlle; Lapicque, Françoise; Drelon, E.; Netter, Patrick

doi:10.1111/j.2042-7158.1994.tb03798.x

Cited by 75 publications

(63 citation statements)

References 16 publications

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“…Based on the molar fluorescence spectra, which are only valid under the conditions and instrument settings applied, stability constants were calculated using PSEQUAD [44]. The conditional HSA binding constants (logK') for WF, BR and DG are comparable with data obtained by us and others [26][27][28][29][30][31][32]36,47,48] (Table S1) accompanied by a considerable decrease in the emission intensity. Therefore, the displacement of the site markers at various concentrations of the Ru(III) complexes could be followed via intensity changes of the emission spectra.…”

Section: Resultsmentioning

confidence: 72%

“…A typical site marker for site I is the anticoagulant drug warfarin (WF) [26][27][28][29], while dansylglycine (DG) shows specificity for site II (see Fig. S1) [30][31][32]. Initial rapid binding of KP1019 takes place in a non-covalent manner at the hydrophobic binding sites of HSA, however after a longer incubation time the type of the interaction is converted slowly to a protein-coordinated form [33].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

et al. 2012

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Indazolium trans-[tetrachloridobis(1H-indazole)ruthenate(III)] (KP1019) and its Na + analogue (KP1339) are two of the most prominent non-platinum antitumor metal complexes currently undergoing clinical trials. After intravenous administration, they are known to bind to human serum albumin (HSA) in a non-covalent manner. In order to elucidate their HSA binding sites, displacement reactions with the established site markers warfarin and dansylglycine as well as bilirubin were monitored by spectrofluorimetry, ultrafiltration−UV-vis spectrophotometry and/or capillary zone electrophoresis. Conditional stability constants for the binding of KP1019 and KP1339 to sites I and II of HSA were determined, indicating that both Ru(III) compounds bind into both sites with moderately to strong affinity (logK 1 ' = 5.3-5.8). No preference for either binding site was found and similar results were obtained for both metal complexes, demonstrating low influence of the counter ion on the binding event.

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Section: Resultsmentioning

confidence: 72%

Section: Introductionmentioning

confidence: 99%

Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

et al. 2012

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“…If the latter is the case, the probe-to-protein molar ratios should be kept well below unity to minimize secondary probe binding. Examples of site I probes, in addition to warfarin, are 5-dimethylaminonaphthalene-1-sulfonamide (DNSA), 6) dansylamide, 40,41) dansyl-L-glutamine, 40) dansyl-Lasparagine, 10) dansyl-L-lysine, 42) n-butyl p-aminobenzoate, 10) prodan, 43) and phenol red, 7) and among the site II probes are dansylsarcosine, 6) dansyl-L-proline, 40) dansylglycine, 41) and 7-alkylaminocoumarin-4-acetic acids. 44) Care should be exercised with respect to site I especially, because, as mentioned above, several examples of independent co-binding of two ligands to this site have been reported.…”

Section: Ligand Bindingmentioning

confidence: 99%

Practical Aspects of the Ligand-Binding and Enzymatic Properties of Human Serum Albumin.

Kragh‐Hansen

Chuang

Otagiri

2002

Biological & Pharmaceutical Bulletin

939

776

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Recent work with approaches like recombinant mutants and X-ray crystallography has given much new information about the ligand-binding properties of human serum albumin (HSA). The information increases the understanding of this unique transport and depot protein and could give a structural basis for the possible construction of therapeutic agents with altered HSA-binding properties. A tabulation of high-affinity binding sites for both endogenous and exogenous compounds has been made; it could be useful for the above-mentioned purpose, but it could also be of value when trying to predict potential drug interactions at the protein-binding level. Drug displacement is not always a complication to therapy; it can be used to increase the biological effect of a drug. However, due to rebinding at other sites, the increase in the free concentration of a displaced ligand can be less than expected. Drugs and drug metabolites can also interact covalently with HSA; thiol-containing drugs often bind to the single free cysteine residue of HSA, and glucuronidated drugs react irreversibly with other residues of the protein. Reversible binding of ligands is often stereospecific, and therefore immobilized HSA can be used to separate drug isomers. Albumin-containing dialysates are useful for extracorporeal removal of endogenous toxins and in the treatment of drug overdoses. HSA has different types of hydrolytic activities, which also can be stereospecific. The esterase-like property seems especially useful in converting prodrugs to active drugs in plasma.

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“…22 Spectrophotometry and fluorometry have been extensively used for direct study of drug-protein interaction based on monitoring the change of a physicochemical property of the drug-protein system. 23,24 Ion-selective electrode and quartz crystal resonant sensor techniques have also been developed for the direct study of drug-protein interaction. 25,26 Each of them often presents different advantages and disadvantages.…”

Section: Introductionmentioning

confidence: 99%

A Study on the Interaction of the DAS‐K with Bovine Serum Albumin by On‐line Ultrafiltration and Chemiluminescence

Zhang

Zhang²,

Sun

2006

Chin. J. Chem.

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Potassium dehydroandrographolide succinate (DAS-K) has antibacterial and antiviral effects. It has been used widely for the treatment of virus pneumonia, malaria and respiratory infections. In this work, a novel flow-injection chemiluminescence (CL) method for the determination of DAS-K was proposed. The method is based on the reaction between DAS-K and hexacyanoferrate(III) in alkaline solution to give weak CL signal, which is enhanced by rhodamine B. The experimental conditions for the CL reaction were optimized and the possible reaction mechanism was discussed. Under the optimum conditions, the concentration of DAS-K is proportional to the CL intensity in the range of 0.1-80 µmol•L -1 with a detection limit of 0.05 µmol•L -1 . The interaction of the DAS-K with bovine serum albumin by on-line ultrafiltration and flow-injection chemiluminescence was studied. The concentrations of unbound DAS-K from ultra filter tube were determined by the flow-injection CL method. The binding parameters were estimated by the Scatchard plot and Klotz plot. The proposed system proved that FIA-CL coupled with on-line ultrafiltration sampling was a fast and simple technique for the study of drug-protein interaction.

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Binding Sites of Fluorescent Probes on Human Serum Albumin

Cited by 75 publications

References 16 publications

Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

Practical Aspects of the Ligand-Binding and Enzymatic Properties of Human Serum Albumin.

A Study on the Interaction of the DAS‐K with Bovine Serum Albumin by On‐line Ultrafiltration and Chemiluminescence

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