Molecular interaction in capillary electrophoresis

Galbusera, Chiara; Chen, David D. Y.

doi:10.1016/s0958-1669(02)00020-4

Cited by 47 publications

(39 citation statements)

References 22 publications

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“…ACE has been applied to study both strong and weak bindings, either by the preequilibration approach (for slow dissociating complexes) or by the migration shift experiments (for fast rate complexations) [35][36][37][38][39]. The second approach is based on mobility changes of the analyte injected, which correlates with the concentration of the species added to the electrophoresis buffer and thus enables the calculation of the binding constant.…”

Section: Acementioning

confidence: 99%

Search of ligands for the amyloidogenic protein β2-microglobulin by capillary electrophoresis and other techniques

et al. 2005

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Beta2-microglobulin (beta2-m) is a small amyloidogenic protein normally present on the surface of most nucleated cells and responsible for dialysis-related amyloidosis, which represents a severe complication of long-term hemodialysis. A therapeutic approach for this amyloidosis could be based on the stabilization of beta2-m through the binding to a small molecule, and consequent inhibition of protein misfolding and amyloid fibril formation. A few compounds have been described to weakly bind beta2-m, including the drug suramin. The lack of a binding site for nonpolypeptidic ligands on the beta2-m structure makes it difficult for both the identification of functional groups responsible for the binding and the search of hits to be optimized. The characterization of the binding properties of suramin for beta2-m by using three different techniques (surface plasmon resonance, affinity CE (ACE), ultrafiltration) is here described and the results obtained are compared. The common features of the chemical structures of the compounds known to bind the protein led us to select 200 sulfonated/suramin-like molecules from a wider chemical library on the basis of similarity rules, so as to possibly single out some interesting hits and to gain more information on the functional groups involved in the binding. The development of screening methods to test the compounds by using ultrafiltration and ACE is described.

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Section: Acementioning

confidence: 99%

Search of ligands for the amyloidogenic protein β2-microglobulin by capillary electrophoresis and other techniques

et al. 2005

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“…32 More elaborate discussions on the prerequisites of mobility shift affinity CE and EKC can be found elsewhere. 3,6,8,[29][30][31]33 Having established the equations appropriate for affinity EKC studies as well as the fundamental practical concerns in brief, it may be timely to ask when it is advantageous to apply EKC instead of the ACE approach. Neubert et al referred to the two closely related approaches, as the partition (distribution) and the association model, respectively.…”

Section: Department Of Pharmaceutics and Analytical Chemistry Facultmentioning

confidence: 99%

“…micelles, microemulsion droplets or liposomes. [3][4][5][6][7][8] Depending on the nature of the constituent added to the background electrolyte, the data analysis procedure may vary. The background electrolyte including the ligand may be considered as a homogenous solution (mobility shift ACE) or as a two-phase system, the additive (ligand) constituting the pseudo-stationary phase.…”

Section: Introductionmentioning

confidence: 99%

Application of Retention Factors in Affinity Electrokinetic Chromatography and Capillary Electrophoresis

Østergaard

2007

ANAL. SCI.

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“…Changes in migration time of the analyte, as a function of ligand concentration, can be used to estimate binding constants. The broad applicability of ACE methods to the study of binding interactions is illustrated by a variety of works on biomolecular interactions [11], such as protein-drug [12], protein-sugar [13], antibody-antigen [14], lectin-sugar [15], protein-or peptidepolymeric materials [16], drug-cyclodextrins [17,18], and drug-DNA [19]. Although many papers have reported ACE for protein-DNA interaction studies [20][21][22][23], very little literature describing dynamic complexation capillary electrophoresis (CE) has focused on these molecular interactions [24,25].…”

Section: Introductionmentioning

confidence: 99%

Poly(ethylene oxide) facilitates the characterization of an affinity between strongly basic proteins with DNA by affinity capillary electrophoresis

et al. 2005

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In order to study kin17 protein-DNA affinity, we have developed a fast and reproducible capillary electrophoresis (CE) analysis of a strongly basic protein: kin17 protein, using a nonpermanent coating based on poly(ethylene oxide) (PEO) to avoid adsorption of kin17. The coating procedure was optimized to provide a residual and stable electroosmotic flow (EOF = 5 x 10(-5) cm(2)/V x s), exhibiting RSD of 0.3% and excellent long-term stability. Good intraday and interday reproducibility of kin17 migration times (0.8 and 0.3% relative standard deviation (RSD), respectively) enabled us to consider that the recovery percentage obtained for kin17 protein was satisfactory (79%). The potential of this PEO-based coating procedure was evaluated for affinity CE method in order to study the affinity of kin17 protein for two single-stranded DNA (ssDNA) models: polydeoxyadenylic acid and polydeoxycytidilic acid (pdA and pdC). Binding constants (1.5 x 10(7) +/- 17% and 1.7 x 10(7) + 25%M(-1)) were evaluated assuming a 1:1 affinity between kin17 and pdA or pdC, respectively.

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Molecular interaction in capillary electrophoresis

Cited by 47 publications

References 22 publications

Search of ligands for the amyloidogenic protein β2-microglobulin by capillary electrophoresis and other techniques

Search of ligands for the amyloidogenic protein β2-microglobulin by capillary electrophoresis and other techniques

Application of Retention Factors in Affinity Electrokinetic Chromatography and Capillary Electrophoresis

Poly(ethylene oxide) facilitates the characterization of an affinity between strongly basic proteins with DNA by affinity capillary electrophoresis

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