Chiral separations by capillary electrophoresis using proteins as chiral selectors.

Abstract

AbstractHigh-performance liquid chromatography (HPLC) chiral stationary phases based on a protein are of special interest because of their unique properties of stereoselectivity and because they are suited for separating a wide range of enantiomeric mixtures. These come from the multiple binding sites in a protein, and/or the multiple interactions between a solute and protein. Similarly, capillary electrophoresis (CE) methods using proteins as the immobilized or adsorbed ligands or running buffer additives have been developed for the separation of enantiomeric mixtures (1–4). Proteins used so far as chiral selectors have included albumins, such as bovine serum albumin (BSA), human serum albumin (HSA), and serum albumins from other species; glycoproteins such as α1-acid glycoprotein (AGP), ovomucoid from chicken egg whites (OMCHI), ovoglycoprotein from chicken egg whites (OGCHI), avidin, and riboflavin-binding protein (or flavoprotein); enzymes, such as fungal cellulase from fungus Aspergillus niger, cellobiohydrolase I, pepsin, and lysozyme; and other proteins such as ovotransferrin (or conalbumin), β-lactoglobulin, casein, and human serum transferrin.KeywordsHuman Serum AlbuminCapillary ElectrophoresisChiral SelectorFuse Silica CapillaryChiral SeparationThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.