Sugar–lectin interactions investigated through affinity capillary electrophoresis

Hong, Mingfang; Cassely, Aaron; Mechref, Yehia; Novotný, Miloš V.

doi:10.1016/s0378-4347(00)00564-8

Cited by 34 publications

(31 citation statements)

References 27 publications

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“…In the life sciences, intermolecular forces between receptor-ligand pairs are of general interest since most biological processes represent a cascade of receptor-ligand recognition events. [3]. Finally, Zhang et al has coupled on-column ligand synthesis to ACE to measure affinities of peptides to receptors [4].…”

Section: Introductionmentioning

confidence: 99%

Determination of binding constants between the antibiotic ristocetin A and D-Ala-D-Ala terminus peptides by affinity capillary electrophoresis

Azad¹,

Hernandez²,

Plazas³

et al. 2003

Chromatographia

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SummaryBinding constants belween the antibiotic ristocetin A (Rist A) and D-Ala-D-Ala terminus peptides were determined using affinity capillary electrophoresis (ACE). In these experiments ~o techniques are used to obtain binding constants. In the first, a plug of RistAand non-interacting standards are injected and electrophoresed. Analysis of the change in the relative migration time ratio (RMTR) of Rist, relative to the non-interacting standards, as a function of the concentration of peptide, yields a value for the binding constant (Kb). In the second, samples of peptide and standards are injected and electrophoresed in increasing concentrations of Rist A in the running buffer. Analysis using the RMTRyields a Kb. The findings described here demonstrate the advantage of using ACE for estimating binding parameters be~een antibiotics and ligands.

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Section: Introductionmentioning

confidence: 99%

Determination of binding constants between the antibiotic ristocetin A and D-Ala-D-Ala terminus peptides by affinity capillary electrophoresis

Azad¹,

Hernandez²,

Plazas³

et al. 2003

Chromatographia

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“…Comparing the binding between concanavalin A (Con A) with various saccharide oligomers (dextrins, dextrans, and N-linked glycans from various glycoproteins), it was found that Con A shows a binding discrimination between the a-(1,6)-linked dextran and a-(1,4)-linked dextrin oligomers. The presence of mannose units at the nonreducing ends of glycans was confirmed to enhance the interaction of glycans with Con A [66]. The interaction between b 2 -microglobulin and polysaccharide was investigated by Heegaard et al [67,68].…”

Section: Protein (Polypeptide)-carbohydrate Interactionmentioning

confidence: 99%

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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“…As these interactions are of intermediate affinity they are very well suited for studies based on mobility shift on-line (or dynamic complexation) ACE [54,[153][154][155][156] yet being of high enough specificity to enable simultaneous elucidation of the carbohydrate structures released from different glycoproteins [157] and to characterize the various carbohydrate structures present in microheterogeneous glycoproteins such as ovalbumin [153]. A detailed study of concanavalin A binding to various oligosaccharides and glycoproteins showed that in addition to the structure of the N-linked glycan core the length of the sugar chain as well as the presence of mannose at the nonreducing ends of the carbohydrate influenced binding [158]. Studies such as these are very difficult to carry out with any other technique.…”

Section: Lipids and Carbohydratesmentioning

confidence: 99%

Applications of affinity interactions in capillary electrophoresis

Heegaard

2003

Electrophoresis

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Capillary electrophoresis (CE) has proven useful for the study of reversible molecular interactions. This is because highly efficient and reproducible separations take place in an environment where molecular interactions may contribute to selectivity without being inhibited by adverse buffer conditions. Affinity CE may be used to estimate quantitative binding data (binding constants and in some cases binding stoichiometries and rate constants) for various molecular interactions. Specific binding interactions (e.g., based on antibodies or aptamers) may also be utilized to quantitatively measure specific analytes using CE. Applications within these areas are here reviewed with focus on the last three years and with emphasis on novel concepts as well as innovative methodology and technology. It is concluded that the affinity CE approach is of growing versatility and will continue to play an integral role in discovering, characterizing, and exploiting biomolecular interactions.

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Sugar–lectin interactions investigated through affinity capillary electrophoresis

Cited by 34 publications

References 27 publications

Determination of binding constants between the antibiotic ristocetin A and D-Ala-D-Ala terminus peptides by affinity capillary electrophoresis

Determination of binding constants between the antibiotic ristocetin A and D-Ala-D-Ala terminus peptides by affinity capillary electrophoresis

Recent advances in the study of biomolecular interactions by capillary electrophoresis

Applications of affinity interactions in capillary electrophoresis

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