Identification, quantitation, and characterization of biomolecules by capillary electrophoretic analysis of binding interactions

The high resolving power of capillary electrophoresis combined with the spe cificity of binding interactions may be used with advantage to characterize the structure-function relationship of biomolecules, to quantitate specifi c analytes in complex sample matrices, and to determine the purity of pharm aceutical and other molecules. We here review recent and innovative methodo logies and applications of high resolution affinity electrophoresis within the fields of binding constant determination, structure-activity studies, q uantitative microassays, analysis of drug purity and protein conformation, and immobilized affinity ligands. Despite the virtues of these approaches w ith respect to applicability, resolving power, speed, and low sample consum ption, problems remain with respect to analyte identification and low conce ntration limits of detection. The ongoing development of new detector techn ologies for capillary electrophoresis such as mass spectrometry, and possib ly nuclear magnetic resonance and other spectroscopic methods, is therefore very promising for the continued increased use of affinity capillary elect rophoresis.