Applications of affinity interactions in capillary electrophoresis

Abstract

Capillary electrophoresis (CE) has proven useful for the study of reversible molecular interactions. This is because highly efficient and reproducible separations take place in an environment where molecular interactions may contribute to selectivity without being inhibited by adverse buffer conditions. Affinity CE may be used to estimate quantitative binding data (binding constants and in some cases binding stoichiometries and rate constants) for various molecular interactions. Specific binding interactions (e.g., based on antibodies or aptamers) may also be utilized to quantitatively measure specific analytes using CE. Applications within these areas are here reviewed with focus on the last three years and with emphasis on novel concepts as well as innovative methodology and technology. It is concluded that the affinity CE approach is of growing versatility and will continue to play an integral role in discovering, characterizing, and exploiting biomolecular interactions.

Quantification of single-stranded nucleic acid and oligonucleotide interactions with metal ions by affinity capillary electrophoresis: part I

“…Affinity capillary electrophoresis (ACE) is a powerful tool for studying DNA-macromolecule interactions [8][9][10] and the simplicity, speed and sensitivity of measurement make it attractive for studying DNA-metal ion interactions. Although ACE investigations of metal ion-DNA interactions have been reported, only a few studies describe the quantification of complex equilibria.…”

Highly Sensitive Methods Using Liquid Chromatography and Capillary Electrophoresis for Quantitative Analysis of Glycoprotein Glycans

“…Affinity capillary electrophoresis (ACE) is a version of CE, and has been used to examine various biological interactions [18][19][20][21][22]. ACE using carbohydrate recognition proteins, such as lectins has certain advantages in the glycobiology era.…”

Characterization of interactions between organotin compounds and human serum albumin by capillary electrophoresis coupled with inductively coupled plasma mass spectrometry

“…ACE method can be performed in physiological solutions to preserve biological interactions between chemical compounds and biomolecules, and is thus more promising than the techniques operated in denaturing mode. In addition, ACE does not suffer from the complication resulting from two-phase chromatographic systems and is therefore particularly suited to study complex formation reactions [12]. NECEEM is another analytical approach, which could also be used to determine the binding constants of the non-covalent interaction between biomolecules and compounds.…”