Estimation of binding constants by capillary electrophoresis

Tanaka, Yoshihide; Terabe, Shigeru

doi:10.1016/s0378-4347(01)00488-1

Cited by 210 publications

(177 citation statements)

References 77 publications

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“…Different modes or formats of affinity CE (ACE) have been developed and are compared in several studies [13,14] and reviews [7][8][9][15][16][17]. Common to the approaches is that the molecular interaction under investigation must alter the size, shape or charge of one of the species to produce a change in the migration pattern [7].…”

Section: Introductionmentioning

confidence: 99%

“…Common to the approaches is that the molecular interaction under investigation must alter the size, shape or charge of one of the species to produce a change in the migration pattern [7]. The strength of the interaction is quantified by migrations shifts (ACE, vacancy ACE) or the measurement of either bound (Hummel-Dreyer) or free ligand concentration (vacancy peak, pre-equilibrium CZE, frontal analysis continuous CE (FACCE), CE-frontal analysis (CE-FA)) [7,13,14,17]. ACE is the most commonly used methodology of the CEbased approaches to interaction studies [17].…”

Section: Introductionmentioning

confidence: 99%

“…The strength of the interaction is quantified by migrations shifts (ACE, vacancy ACE) or the measurement of either bound (Hummel-Dreyer) or free ligand concentration (vacancy peak, pre-equilibrium CZE, frontal analysis continuous CE (FACCE), CE-frontal analysis (CE-FA)) [7,13,14,17]. ACE is the most commonly used methodology of the CEbased approaches to interaction studies [17]. CE-FA has attracted less attention and may as a method possess a higher unexploited development potential.…”

Section: Introductionmentioning

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: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

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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“…Affinity capillary electrophoresis (ACE) is a version of CE, and has been used to examine various biological interactions [18][19][20][21][22]. ACE using carbohydrate recognition proteins, such as lectins has certain advantages in the glycobiology era.…”

Section: Partial Filling Affinity Capillary Electrophoresis For Glycamentioning

confidence: 99%

Highly Sensitive Methods Using Liquid Chromatography and Capillary Electrophoresis for Quantitative Analysis of Glycoprotein Glycans

Suzuki

2014

Chromatography

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This review summarizes our recent works concerned on the analysis of glycoprotein glycans. Glycoprotein glycans are highly complicated and have variations that number into the thousands. Therefore the method for their analyses should be carefully chosen according to the complexity and quantity of glycans in samples. To shorten the time for the preparation of labeled glycans from glycoprotein, we proposed two methods: PNGase F/NBD-F method enables the preparation of fluorescently labeled glycans from glycoproteins about 2 hr. A combination of a neutrally coated capillary and borate buffer eliminates the purification steps for the removal of excess reagents from the glycan samples for capillary electrophoresis. Partial filling affinity capillary electrophoresis using glycan-recognizing proteins such as lectins, glycosidases and immunoglobulins, was used for the structural analysis of glycans. The method was applied to the specific detection of NeuGc and α-Gal containing glycans known as the heterogenic antigens. Sensitivity of the detection of glycoprotein glycans separated by microchip-based electrophoresis was enhanced by in situ fabricated sufonate-type polyacrylamide gel. This method enhances the sensitivity by a factor of 10 5 . In situ fabrication of lectin impregnated gels enables specific entrapment and analysis of glycans. Conversion reaction from fluorescently labeled glycans (1-amino-1-alditols) to free oligosaccharides will be helpful for the functional analysis of glycans.

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“…[10][11][12] ACE has several advantages, besides its speed and flexibility: a) only a small amount of protein and drug is required; b) non-purified sample can be injected directly; c) binding constants of several samples can be simultaneously estimated; d) all interaction components can be studied in free buffer solution at so-called physiological conditions.…”

Section: Introductionmentioning

confidence: 99%

Interaction between Fluoroquinolones and Bovine Serum Albumin Studied by Affinity Capillary Electrophoresis

Liu

Zhang

2006

ANAL. SCI.

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The interactions between eight fluoroquinolone antibiotics (ciprofloxacin, enoxacin, fleroxacin, levofloxacin, lomefloxacin, norfloxacin, ofloxacin, pefloxacin) and bovine serum albumin (BSA) were studied by affinity capillary electrophoresis (ACE). The binding constants were estimated by the change of migration times of the analytes through the change of concentration of BSA in the buffer solution. The yield binding constants were between 3.19 × 10 4 and 1.21 × 10 5 M -1 . These were related with the structures of fluoroquinolones, and agreed with the results obtained by other techniques. The obtained binding constants may help us in gaining some insights on possible drug/protein interactions and in early evaluation of the drugs' pharmacokinetic profiles during drug discovery.

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Estimation of binding constants by capillary electrophoresis

Cited by 210 publications

References 77 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

Highly Sensitive Methods Using Liquid Chromatography and Capillary Electrophoresis for Quantitative Analysis of Glycoprotein Glycans

Interaction between Fluoroquinolones and Bovine Serum Albumin Studied by Affinity Capillary Electrophoresis

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