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This version was published on March 1, 2006
Journal of Biomolecular Screening, Vol. 11, No. 2, 115-122 (2006)
DOI: 10.1177/1087057105284339

Nonequilibrium Capillary Electrophoresis of Equilibrium Mixtures (NECEEM): A Novel Method for Biomolecular Screening

Sergey N. Krylov

Department of Chemistry, York University, Toronto, Ontario, Canada

Nonequilibrium capillary electrophoresis of equilibrium mixtures (NECEEM) is a new separation-based affinity method. It has kinetic capabilities exceeding those of surface plasmon resonance (SPR) and does not require immobilization of molecules on the surface. Another distinctive feature of NECEEM is that—if it is combined with an advanced method for the mixing solutions inside a capillary, termed transverse diffusion of laminar flow profiles (TDLFP)—it requires only nanoliter volumes of solutions. The proven applications of NECEEM to biomolecular screening include 1) measuring kinetic and thermodynamic parameters of protein-ligand interactions, 2) quantitative affinity analyses of proteins and hybridization analyses of DNA and RNA, and 3) selection of binding ligands from combinatorial libraries. NECEEM is easy to automate and parallelize. Because of its simplicity and analytical power, NECEEM has the potential to become a workhorse in studies of biomolecular interactions. The author reviews theoretical bases of NECEEM and its applications to biomolecular screening.

Key Words: affinity methods • kinetic capillary electrophoresis (KCE) • nonequilibrium capillary electrophoresis of equilibrium mixtures (NECEEM) • rate constants • selection • aptamers


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