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Updated: Jul 18, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
Published on: February 18, 2014
Analysis of cholinesterase binding to a carnitine-modified EQCM sensor
Jiri Zeravik1, Carsten Teller, Frieder W Scheller
1Department of Analytical Biochemistry, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Strasse 24-25, 14476 Golm, Germany. zeravik@uni-potsdam.de
Abstract:
A sensor for cholinesterases (ChEs) has been developed by binding carnitine via 1,6-diaminohexane to a mixed monolayer of 11-mercaptoundecanoic acid/11-mercapto-1-undecanol on the surface of a gold-coated quartz crystal. Catalytically active and organophosphate-inhibited acetyl- and butyryl-cholinesterases of different origins were tested for their binding ability to D- and L-carnitine, respectively. The binding constants were calculated by using a one-to-one binding model. Additionally, the activity of the immobilized ChE was monitored and the operational stability was investigated amperometrically.
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