Evalution of capillary electrophoresis-frontal analysis for the study of low molecular weight drug-human serum albumin interactions

Østergaard, Jesper; Schou, C.; Larsen, Claus; Heegaard, Niels H. H.

doi:10.1002/1522-2683(200209)23:17<2842::aid-elps2842>3.0.co;2-b

Cited by 78 publications

(85 citation statements)

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“…Both warfarin and HSA are negatively charged at pH 7.4. It has been shown that the electrophoretic mobility of HSA is not changed significantly upon binding of low-molecular-weight ligands such as warfarin [34], thus, the mobility of free protein and complex can be considered to be equal. As separation progresses free warfarin, warfarin-HSA complex, and HSA are swept towards the detector by the EOF.…”

Section: Principles Of Capillary Electrophoresisfrontal Analysis (Ce-fa)mentioning

confidence: 78%

“…Otherwise determination of the free ligand concentrations is not feasible. In the case above, the mobility of warfarin changes upon binding while that of HSA is unchanged [34]. Recently, we have addressed the necessity of having plateau peak conditions in CE-FA experiments (Østergaard and Hansen, manuscript in preparation).…”

Section: Requirements For Using Ce-famentioning

confidence: 85%

“…Examples include the binding of warfarin to BSA [13,14] and L-tryptophan, warfarin, ibuprofen, and flurbiprofen binding to HSA [38][39][40]. Furthermore, results obtained by CE-FA appear to be in good accordance with other methods, e.g., [14,34,36,[41][42][43]. CE-FA, being a pre-equilibrium method differs mainly from preequilibrium CZE [44][45][46] and FACCE [47] with respect to the sample volume introduced into the capillary.…”

Section: Requirements For Using Ce-famentioning

confidence: 99%

“…Otherwise the free concentrations determined would be associated with an error. Experiments strongly indicate that low-molecular-weight ligand-HSA [34], drug-a 1 -acid glycoprotein (AGP) [48][49][50][51], and drug-lipoprotein [41] binding fulfil these requirements. The order of magnitude of the errors arising from not complying with the mobility restrictions has not been assessed.…”

Section: Requirements For Using Ce-famentioning

confidence: 99%

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Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

2003

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Capillary electrophoresis frontal analysis: Principles and applications for the study of drug-plasma protein bindingCapillary electrophoresis is a well-established technique for the study of noncovalent interactions. Various approaches exist and capillary electrophoresis-frontal analysis provides an interesting alternative to the migration shift affinity capillary electrophoresis methods and conventional methods. The present work reviews the principles on which the frontal analysis method is founded. Advantages and limitations of capillary electrophoresis frontal analysis in comparison with both conventional and other capillary electrophoresis based methods for quantification of binding interactions are discussed. Investigations utilizing capillary electrophoresis-frontal analysis have focused on the interaction of drugs with plasma proteins. These studies, primarily addressing the binding of drugs to human serum albumin, a 1 -acid glycoprotein, and lipoproteins are reviewed together with some recent developments in capillary electrophoresisfrontal analysis methodology.

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Section: Principles Of Capillary Electrophoresisfrontal Analysis (Ce-fa)mentioning

confidence: 78%

Section: Requirements For Using Ce-famentioning

confidence: 85%

Section: Requirements For Using Ce-famentioning

confidence: 99%

Section: Requirements For Using Ce-famentioning

confidence: 99%

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Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

2003

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“…50 We elected to evaluate the impact of treating bile duct-cannulated rodents with sodium benzoate to displace any chelator potentially bound to Sudlow type I and II albumin binding sites. 50 Five experiments were carried out (Table 4). Rodents were given (i) sodium benzoate dissolved in distilled water at 250 mg/kg/dose sc times six doses, (ii) (S)-4′-(HO)-DADFT (1) po at 300 μmol/kg, (iii) 1 given po at 300 μmol/kg plus sodium benzoate (250 mg/kg/dose).…”

Section: The Possible Impact Of Ligand-albumin Binding On Icementioning

confidence: 99%

Impact of the 3,6,9-Trioxadecyloxy Group on Desazadesferrithiocin Analogue Iron Clearance and Organ Distribution

et al. 2007

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The impact of introducing a 3,6,9-trioxadecyloxyl group at various positions of the desazadesferrithiocin (DADFT) aromatic ring on iron clearance and organ distribution is described. Three DADFT polyethers are evaluated: (S)-4,5-dihydro-2- [2-hydroxy-4-(3,6,9- trioxadecyloxy) phenyl]-4-methyl-4-thiazolecarboxylic acid [(S)-4′-(HO)-DADFT-PE, 3], (S)-4,5-dihydro-2-[2-hydroxy-5-(3,6,9-trioxadecyloxy)phenyl]-4-methyl-4-thiazolecarboxylic acid [(S)-5′-(HO)-DADFT-PE, 6], and (S)-4,5-dihydro-2-[2-hydroxy-3-(3,6,9-trioxadecyloxy)phenyl]-4-methyl-4-thiazolecarboxylic acid [(S)-3′-(HO)-DADFT-PE, 9]. The iron-clearing efficiency (ICE) in rodentsand primates is shown to be very sensitive to which positional isomer is evaluated, as is the organ distribution in rodents. The polyethers had uniformly higher ICE than their corresponding parent ligands in rodents, consistent with in vivo ligand-serum albumin binding studies. Ligand 9 is the most active polyether analogue in rodents and is also very effective in primates, suggesting a higher index of success in humans. In addition, this analogue is also shown to clear more iron in the urine of the primates than many of the other chelators. If this trend were also observed in patients, it would facilitate iron-balance studies in a clinical setting.Humans have evolved a highly efficient iron management system in which we absorb and excrete only about 1 mg of the metal daily; there is no mechanism for the excretion of excess iron. 1 Whether derived from transfused red blood cells 2-4 or from increased absorption of dietary iron, 5,6 without effective treatment, body iron progressively increases with deposition in the liver, heart, pancreas, and elsewhere. Iron accumulation eventually produces (i) liver disease that may progress to cirrhosis, 7-9 (ii) diabetes related both to iron-induced decreases in pancreatic β-cell secretion and increases in hepatic insulin resistance, 10,11 and (iii) heart disease, still the leading cause of death in thalassemia major and related forms of transfusional iron overload. 1,12,13Although iron comprises 5% of the earth's crust, living systems have great difficulty in accessing and managing this vital micronutrient. The low solubility of Fe(III) hydroxide (K sp = 1 × 10 −39 ), 14 the predominant form of the metal in the biosphere, has led to the development of sophisticated iron storage and transport systems in nature. Microorganisms utilize low molecular weight, virtually ferric ion-specific, ligands, siderophores; 15,16 higher eukaryotes tend to employ proteins to transport and store iron (e.g., transferrin and ferritin, respectively). 17-19 In humans, nontransferrin-bound plasma iron, a heterogeneous pool of iron *Corresponding Author: Raymond J. Bergeron, Ph.D., Box 100485 JHMHSC, Department of Medicinal Chemistry, University of Florida, Gainesville, Florida 32610-0485, Phone (352) 846-1956, Fax (352) in the circulation that is not bound to the physiological iron transporter, transferrin, seems to be a principal source of iron-mediated o...

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Characterization of interactions between methoxatin disodium salt and human serum albumin by pressure‐assisted capillary electrophoresis/frontal analysis and circular dichroism spectroscopy

Zhao

Chen

2014

Biomedical Chromatography

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Pressure-assisted capillary electrophoresis (PACE)/frontal analysis (FA) and circular dichroism spectroscopy were utilized to investigate the interactions between methoxatin disodium salt (PQQ-2Na) and human serum albumin (HSA). With the PACE/FA method, sodium phosphate buffer solution (67 mm, pH 7.4) was used as the background electrolyte. Hydrodynamic injection at 50 mbar for 50 s and external pressure of 50 mbar were applied. The binding constant and the number of primary binding sites to HSA were obtained under fixed concentration of PQQ-2Na (100 µm) and increasing HSA concentration (0~475 µm). The thermodynamic parameters characterized the main acting forces of hydrophobic and electrostatic interactions. The displacement experiments using phenylbutazone and flurbiprofen as ligand markers suggested that the binding site was the Sudlow site I of the HSA molecule. Circular dichroism spectroscopy was further employed to evaluate the conformation changes of HSA under the interaction of PQQ-2Na. This work provides comprehensive information for understanding the interactions between PQQ-2Na and HSA.

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Evalution of capillary electrophoresis-frontal analysis for the study of low molecular weight drug-human serum albumin interactions

Cited by 78 publications

References 64 publications

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

Capillary electrophoresis frontal analysis: Principles and applications for the study of drug‐plasma protein binding

Impact of the 3,6,9-Trioxadecyloxy Group on Desazadesferrithiocin Analogue Iron Clearance and Organ Distribution

Characterization of interactions between methoxatin disodium salt and human serum albumin by pressure‐assisted capillary electrophoresis/frontal analysis and circular dichroism spectroscopy

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