Recent advances in the study of biomolecular interactions by capillary electrophoresis

He, Xinya; Ding, Yongsheng; Li, Dazhi; Lin, Bingcheng

doi:10.1002/elps.200305727

Cited by 95 publications

(71 citation statements)

References 158 publications

(166 reference statements)

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“…Based on the stability of the complex, reported ACE methods in capillary zone electrophoresis may be classified into two distinct modes [13,14]. Pre-equilibrium mixture analysis [12,[15][16][17][18]: The complex is formed by pre-incubating the analyte and the binding probe, and then the resulting equilibrium mixture is analyzed under non-equilibrium separation conditions based on electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

Protein‐aptamer binding studies using microchip affinity capillary electrophoresis

et al. 2008

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The use of traditional capillary electrophoresis (CE) to detect weak binding complexes is problematic due to the fast-off rate resulting in the dissociation of the complex during the separation process. Additionally, proteins involved in binding interactions often nonspecifically stick to the bare-silica capillary walls, which further complicates the binding analysis. Microchip CE allows flexibly positioning the detector along the separation channel and conveniently adjusting the separation length. A short separation length plus a high electric field enables rapid separations thus reducing both the dissociation of the complex and the amount of protein loss due to nonspecific adsorption during the separation process. Thrombin and a selective thrombinbinding aptamer were used to demonstrate the capability of microchip CE for the study of relatively weak binding systems that have inherent limitations when using the migration shift method or other CE methods. The rapid separation of the thrombin-aptamer complex from the free aptamer was achieved in less than 10 s on a single-cross glass microchip with a relatively short detection length (1.0 cm) and a high electric field (670 V/cm). The dissociation constant was determined to be 43 nM, consistent with reported results. In addition, aptamer probes were used for the quantitation of standard thrombin samples by constructing a calibration curve, which showed good linearity over two orders of magnitude with a limit of detection for thrombin of 5 nM at a 3-fold signal-to-noise ratio.

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Section: Introductionmentioning

confidence: 99%

Protein‐aptamer binding studies using microchip affinity capillary electrophoresis

et al. 2008

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“…Affinity capillary electrophoresis (ACE) is a powerful tool for studying DNA-macromolecule interactions [8][9][10] and the simplicity, speed and sensitivity of measurement make it attractive for studying DNA-metal ion interactions. Although ACE investigations of metal ion-DNA interactions have been reported, only a few studies describe the quantification of complex equilibria.…”

Section: Introductionmentioning

confidence: 99%

Quantification of single-stranded nucleic acid and oligonucleotide interactions with metal ions by affinity capillary electrophoresis: part I

et al. 2006

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“…CE has been established as an efficient micromethod for studying molecular interactions [23][24][25][26][27][28]. Different formats for conducting affinity CE have been developed; their pros and cons have been discussed previously [23,26,[29][30][31][32][33].…”

Section: Introductionmentioning

confidence: 99%

Binding of Low-Molecular-Weight Cationic Ligands to Chondroitin Sulfate as Studied by Capillary Electrophoresis Frontal Analysis

Østergaard

Jensen²,

Larsen³

et al. 2009

TOACJ

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The feasibility of capillary electrophoresis frontal analysis for the study of low-molecular-weight ligandchondroitin sulfate interactions was investigated. The interaction of the 7 cationic ligands (lidocaine, propranolol, scopolamine, N-methyl scopolamine, N-butyl scopolamine, 2-propylisochinolinium, and methyl viologen) with the glycosaminoglycan chondroitin sulfate was investigated in 0.067 M phosphate buffer, pH 7.4, at 25 o C. A frontal analysis method with a short analysis time, suitable for ranking ligands according to degree of complexation for chondroitin sulfate was developed. The double charged ligand methyl viologen possessed the highest affinity for chondroitin sulfate. Linear binding isotherms were obtained and apparent association constants were determined. Capillary electrophoresis frontal analysis may be an attractive tool for characterization of ligand-glycosaminoglycan interactions.

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Recent advances in the study of biomolecular interactions by capillary electrophoresis

Cited by 95 publications

References 158 publications

Protein‐aptamer binding studies using microchip affinity capillary electrophoresis

Protein‐aptamer binding studies using microchip affinity capillary electrophoresis

Quantification of single-stranded nucleic acid and oligonucleotide interactions with metal ions by affinity capillary electrophoresis: part I

Binding of Low-Molecular-Weight Cationic Ligands to Chondroitin Sulfate as Studied by Capillary Electrophoresis Frontal Analysis

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