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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
Published on: September 7, 2011
Affinity capillary electrophoresis and isothermal titration calorimetry for the determination of fatty acid binding
Kevin M Parker1, Apryll M Stalcup
1Department of Chemistry, University of Cincinnati, Cincinnati, OH 45221-0172, USA. parkerkm@email.uc.edu
Abstract:
Affinity capillary electrophoresis (ACE) and isothermal titration calorimetry (ITC) were used to investigate the binding interaction between several fatty acids (FAs) and beta-cyclodextrin (beta-CD). Within each method, steps taken to obtain accurate binding constants are discussed. The stoichiometry of interaction was revealed to be 1:1 regardless of FA chain length. The binding constants obtained using ACE were: octanoate, 6.4x10(2); 2-octenoate, 4.7x10(2); decanoate, 3.7x10(3); 9-decenoate, 1.8x10(3) and dodecanote, 1.4x10(4). The binding constants obtained from ITC were of the same order of magnitude, but were consistently greater than those from ACE. Thermodynamic data obtained using ITC are used to explain the observed trends in binding strength.
