Study of protein-drug binding using capillary zone electrophoresis

Kraak, J.C.; Busch, Sandra; Poppe, H.

doi:10.1016/0021-9673(92)87132-r

Cited by 197 publications

(127 citation statements)

References 17 publications

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“…The method can be applied over a very wide pH range (pH [1][2][3][4][5][6][7][8][9][10][11][12][13][14], and be operated with aqueous media. Therefore, CE is suited to study almost any biomolecular interaction system.…”

Section: Discussionmentioning

confidence: 99%

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Recent advances in the study of biomolecular interactions by capillary electrophoresis

Ding

et al. 2004

Electrophoresis

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Recent advances in the study of biomolecular interactions by capillary electrophoresisCapillary electrophoresis (CE) has been abundantly used in the study of molecular interactions owing to such advantages as short analysis time, low sample size requirement, high separation efficiency, and flexible applications. The focus of this paper is to review recent studies and advances (mainly from 1998 to now) in biomolecular interactions using CE. Five CE modes: zone migration CE, affinity CE, frontal analysis (FA), Hummel-Dreyer (HD) and vacancy peak (VP) are cited and compared. Quantitative aspects of the thermodynamics and kinetics of biomolecular interaction are reviewed. Several biomolecular binding systems, including protein-protein (polypeptide), protein-DNA (RNA), protein(polypeptide)-carbohydrate, protein-small molecule, DNAsmall molecule, small molecule-small molecule, have been well characterized by CE. CE is shown to be a powerful tool for the determination of the binding parameters of various bioaffinity interactions.

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Section: Discussionmentioning

confidence: 99%

“…Besides, Joule heat, high electric field, wall effect, and properties of the running buffer may also influence the migration of analytes to some extent [18]. In studies of molecular interactions, different CE modes, equipments, or even differences in ligand or receptor concentrations may cause quantitative discrepancies [19][20][21].…”

Section: Area or Heightmentioning

confidence: 99%

Recent advances in the study of biomolecular interactions by capillary electrophoresis

Ding

et al. 2004

Electrophoresis

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“…The negative peak emerged at the migration time of the ligand and the area of that peak was directly related to the amount of ligand bound to the protein, [D b ] (Busch et al, 1997b). The amount of bound ligand was quantified from an external calibration (Sebille et al, 1978;Kraak et al, 1992).…”

Section: Binding Measurementsmentioning

confidence: 99%

Binding of an Oxindole Alkaloid from Uncaria tomentosa to Amyloid Protein (Aβ1-40)

Frąckowiak

Bączek

Kaliszan

et al. 2006

Zeitschrift Für Naturforschung C

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The primary aim of this work was to determine the interactions of an oxindole alkaloid (mitraphylline) isolated from Uncaria tomentosa with -amyloid 1-40 (A 1-40 protein) applying the capillary electrophoresis (CE) method. Specifically the Hummel-Dreyer method and Scatchard analysis were performed to study the binding of oxindole alkaloids with A 1-40 protein. Prior to these studies extraction of the alkaloid of interest was carried out. Identification of the isolated alkaloid was performed by the use of thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC) combined with electrospray ionization mass spectrometry (ESI-MS). The proposed approach was proved to be an efficient and accurate method for specific compound isolation and identification purposes. Moreover, analytical information from the CE approach can be considered as the valuable tool for binding constant determination. The binding constant of mitraphylline with A 1-40 protein determined by the Hummel-Dreyer method and Scatchard analysis equals K = 9.95 ¥ 10 5 m Ð1. The results obtained showed the significant binding of the tested compound with A 1-40 protein.These results are discussed and interpreted in the view of developing a strategy for identification of novel compounds of great importance in Alzheimer disease therapy.

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“…The principle of FA in CE is based on the separation of ligand from protein and proteinligand complex [13,23]. A larger volume of sample solution than normal is introduced into the capillary.…”

Section: Introductionmentioning

confidence: 99%

Frontal analysis in microchip CE: A simple and accurate method for determination of protein–DNA dissociation constant

et al. 2007

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Equilibrium constants, such as the dissociation constant (K d ), are a key measurement of noncovalent interactions that are of importance to the proper functioning of molecules in living systems. Frontal analysis (FA) is a simple and accurate capillary electrophoresis (CE) method for the determination of K d . Microchip CE coupled with laser-induced fluorescence (LIF) detection was used to determine K d of protein-DNA interactions using the FA method. A model system of immunoglobulin E (IgE) and the IgE-binding aptamer was selected to demonstrate the capability of FA in microchip CE. Because the fluorescence emission was dependent on the dye migration velocity, the velocity of the free aptamer was adjusted to be the same as that of the aptamer-IgE complex by setting up individual separation voltage configurations for the free and bound aptamers. The ratio of the free and bound aptamers in the equilibrium mixture was directly measured from the heights of their plateaus detected at 1.0 cm from the intersection of the microchip, and no internal standard was needed. The K d of the IgE-aptamer pair was determined as 6 ± 2 nM which is consistent with the reported results (8 nM).

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Study of protein-drug binding using capillary zone electrophoresis

Cited by 197 publications

References 17 publications

Recent advances in the study of biomolecular interactions by capillary electrophoresis

Recent advances in the study of biomolecular interactions by capillary electrophoresis

Binding of an Oxindole Alkaloid from Uncaria tomentosa to Amyloid Protein (Aβ1-40)

Frontal analysis in microchip CE: A simple and accurate method for determination of protein–DNA dissociation constant

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