Survey of the year 2004: literature on applications of isothermal titration calorimetry

Abstract

The market for commercially available isothermal titration calorimeters continues to grow as new applications and methodologies are developed. Concomitantly the number of users (and abusers) increases dramatically, resulting in a steady increase in the number of publications in which isothermal titration calorimetry (ITC) plays a role. In the present review, we will focus on areas where ITC is making a significant contribution and will highlight some interesting applications of the technique. This overview of papers published in 2004 also discusses current issues of interest in the development of ITC as a tool of choice in the determination of the thermodynamics of molecular recognition and interaction.

Thermodynamic Study of Interactions Between ZnO and ZnO Binding Peptides Using Isothermal Titration Calorimetry

“…16,[23][24][25] Though the use of ITC to study biotic-abiotic interactions is in its infancy it has great potential as it does not require labelling or immobilization of the interacting components and more exceptionally, it can directly measure molar enthalpy of interaction and determine all thermodynamic parameters (enthalpy change (∆H), entropy change (∆S), KA and ∆G) in a single experiment. 26,27 Using ITC, the interaction of the studied ZnO-BPs with ZnO is seen to be an energetically favourable process and is described to involve different events some of which may be occurring simultaneously i.e. peptide-solvent, substrate-solvent, peptide-surface, possible conformation changes between bound and free peptide states and peptide-peptide interactions.…”

Water-Soluble Calix[4]arene Derivatives: Binding Stoichiometry and Spectroscopic Evaluation of the Host-Guest Recognition Mechanism

“…20,21,22 The gradient of the ITC curve can be fitted to determine the binding constant and ΔG complex . Integration of the total area under the ITC plot gives the complexation enthalpy (ΔH complex )which allows for all the system thermodynamic parameters evaluation, being ΔG complex = ΔH complex -TΔS complex .…”

A survey of the year 2007 literature on applications of isothermal titration calorimetry

“…pK a changes are easily detected by ITC if ∆H A is measured as a function of the ionization enthalpy of the buffer (∆H buf ) and the data are plotted according to ∆H A = ∆H bind + n H+ ∆H buf . The slope yields the number of proton(s), n H+ , being taken up or released, and the intercept, ∆H bind , is the protonation-independent binding enthalpy [1]. Still, it is important to keep in mind that ∆G A , ∆H A and ∆S A are apparent parameters, and any discussion of their magnitude and any interpretations invoking details on the underlying physical process should be made with caution.…”

“…There are many in-depth reviews covering the theoretical foundation of ITC, the practical aspects of the method, and the information content of the determined binding parameters [1][2][3][4][5][6][7].…”