Synthesis and characterization of β-CD derivatized bovine serum albumin protein as chiral selector in pressurized capillary electrochromatography

The synthesis and characterization of β-cyclodextrin derivatized bovine serum albumin (β-CD-BSA) as chiral selector in pressurized capillary electrochromatography were investigated in this article. β-CD-BSA was synthesized by crosslinking β-cyclodextrin and BSA using ethylene glycol diglycidyl ether in boric acid buffer at pH 8.7. The internal surface of the fused silica capillary was coated with amino groups using triethoxylmethylsiloxane and (3-aminopropyl)trimethoxysiloxane by sol-gel technology. Then the inner surface of the capillary was further changed to aldehyde groups surface after being treated using glutaraldehyde. β-CD-BSA aqueous solution was pumped in to the capillary, and β-CD-BSA was successfully covalently bonded to the inner surface of the capillary. Chlorpheniramine, phenylalanine, tryptophan, and ibuprofen were separated by β-CD-BSA modified capillary. The operation voltage has certain effect on the separation of the enantiomers. The data showed that higher operation voltage resulted in good separation of tryptophane. However, when the other chiral selectors, β-CD and BSA were employed, the racemic tryptophan was not separated. This indicated that a good chiral separation was obtained when β-CD-BSA was used as chiral selector.