TY - JOUR

T1 - Applications of on-line weak affinity interactions in free solution capillary electrophoresis.

AU - Heegaard, Niels H H

AU - Nissen, Mogens H

AU - Chen, David D Y

N1 - Keywords: Animals; Electrophoresis, Capillary; Humans; Solutions

PY - 2002

Y1 - 2002

N2 - The impressive selectivity offered by capillary electrophoresis can in some cases be further increased when ligands or additives that engage in weak affinity interactions with one or more of the separated analytes are added to the electrophoresis buffer. This on-line affinity capillary electrophoresis approach is feasible when the migration of complexed molecules is different from the migration of free molecules and when separation conditions are nondenaturing. In this review, we focus on applying weak interactions as tools to enhance the separation of closely related molecules, e.g., drug enantiomers and on using capillary electrophoresis to characterize such interactions quantitatively. We describe the equations for binding isotherms, illustrate how selectivity can be manipulated by varying the additive concentrations, and show how the methods may be used to estimate binding constants. On-line affinity capillary electrophoresis methods are especially valuable for enantiomeric separations and for functional characterization of the contents of biological samples that are only available in minute quantities.

AB - The impressive selectivity offered by capillary electrophoresis can in some cases be further increased when ligands or additives that engage in weak affinity interactions with one or more of the separated analytes are added to the electrophoresis buffer. This on-line affinity capillary electrophoresis approach is feasible when the migration of complexed molecules is different from the migration of free molecules and when separation conditions are nondenaturing. In this review, we focus on applying weak interactions as tools to enhance the separation of closely related molecules, e.g., drug enantiomers and on using capillary electrophoresis to characterize such interactions quantitatively. We describe the equations for binding isotherms, illustrate how selectivity can be manipulated by varying the additive concentrations, and show how the methods may be used to estimate binding constants. On-line affinity capillary electrophoresis methods are especially valuable for enantiomeric separations and for functional characterization of the contents of biological samples that are only available in minute quantities.

U2 - 10.1002/1522-2683(200203)23:6<815::AID-ELPS815>3.0.CO;2-V

DO - 10.1002/1522-2683(200203)23:6<815::AID-ELPS815>3.0.CO;2-V

M3 - Journal article

C2 - 11920866

VL - 23

SP - 815

EP - 822

JO - Electrophoresis

JF - Electrophoresis

SN - 0173-0835

IS - 6

ER -