Isothermal titration calorimetry applications

Ladbury, J.E. (2001) Isothermal titration calorimetry Application to structure-based drag design,... 

Another area where titration calorimetry has found intensive application, and where the importance of heat flow versus isoperibol calorimetry has been growing, is the energetics of metal-ligand complexation. Morss, Nash, and Ensor [225], for example, used potenciometric titrations and heat flow isothermal titration calorimetry to study the complexation of UO "1" and trivalent lanthanide cations by tetrahydrofuran-2,3,4,5-tetracarboxylic acid (THFTCA), in aqueous solution. Their general goal was to investigate the potential application of THFTCA for actinide and lanthanide separation, and nuclear fuels processing. The obtained results (table 11.1) indicated that the 1 1 complexes formed in the reaction (M = La, Nd, Eu, Dy, andTm)... 

Ladbury JE (2004) Application of isothermal titration calorimetry in the biological sciences things are heating up . Biotechniques 37(6) 665-687 Leung DH, Bergman RG, Raymond KN (2008) Enthalpy-entropy compensation reveals solvent reorganization as a driving force for supramolecular encapsulation in water. 1 Am Chem Soc... 

Application of Isothermal Titration Calorimetry to Thermodynamic Studies of Biomolecular Interactions. 

The energetics of protein association can be studied by a variety of experimental techniques,17 each of which permits measurements of equilibrium or kinetic values in a certain range. Widely used techniques include isothermal titration calorimetry, surface plasmon resonance measurement, stopped flow kinetics, optical spectroscopy, MS, and analytical ultracentrifugation. The techniques differ in their requirements (e.g., amount of protein, labeling with fluorophores, attachment to sensor surfaces, and the environment provided by the experimental set up) and therefore in their applicability to individual cases. Different techniques can also give quite different values for what might be expected to be the same quantity. For example, association rates measured by surface plasmon resonance, with one protein immobilized on a surface, are usually different from those measured for the two proteins in solution and under otherwise similar conditions. 

A survey of the year 2002 hteramre on applications of isothermal titration calorimetry. J. Mol. Recognit. 16. 383-391. 

The existence of a very large ACp is one possible reason for the value of A7/ of +58.6kJmol obtained by application of the van t Hoff equation, eqn. (5.33), to measured for the inhibition of almond p-glucosidase by isofagomine" which differed even in sign from the value measured directly by isothermal titration calorimetry. ... 

Ladbury, J. E., and Chowdhry, B. Z. (1996). Sensing the heat The application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions. Chem. Biol. 3(10), 791-801. 

Several applications of isothermal titration calorimetry to biochemical systems have been published recently. Franghanel et al. [240] proposed a new calorimetric method to investigate slow conformational changes in proteins and peptides, Tsamaloukas et al. [241] studied the interactions of cholesterol with unsaturated phospholipids and D Amico et al. [242] determined the binding enthalpies of a-amylases to different substrates. 

Isothermal titration calorimetry (ITC) has gained much attention recently, as the application of thermodynamic data in the lead generation process has been proposed as a strategy both to improve the quality of lead series and to allow for a more effective lead optimization process [30-32]. The technique enables the determination of the affinity, the binding enthalpy, and the stoichiometry in a single experiment within a time frame of <1 h using as littie as 100 pg of a target protein. 

Adapted from Steinmann, W., Walter, S., Beckers, M., Seide G., Gries, T., 2013. Thermal analysis of phase transitions and crystallization. In Elkordy A.A. (Ed.), Polymeric Fibers, Applications of Calorimetry in a Wide Context— Differential Scanning Calorimetry, Isothermal Titration Calorimetry and Microcalorimetry. ISBN 978-953-51-0947-1. InTech. Rijeka, pp. 277-306. Available from http //www.intechopen.com (accessed 7.7.15). 

Velazquez-Campoy, A., Leavitt, S. A. and Freire, E. Characterization of protein-protein interactions by isothermal titration calorimetry. In Methods in Molecular Biology Protein-Protein Interactions. Methods and Applications, (H. Fu, ed.), Humana Press Inc., Totowa, New Jersey, pp. 35-54, 2004. 

In the first part of this chapter we will briefly discuss the nature of noncovalent interactions, followed by an overview of standard methods for probing them (optical and fluorescence spectroscopy, isothermal titration calorimetry/microcalorimetry, differential scanning calorimetry, and surface plasmon resonance), with particular attention to their application to biomolecules. An overview of mass spectrometric methods suitable for detecting noncovalent complexes will then be presented. The advantages of mass spectrometry compared with conventional analytical methods are sensitivity, speed, and the ability to obtain stoichiometric information directly. 

Ghai, R., Ealconer, R.J., Collins, B.M. Applications of isothermal titration calorimetry in pure and applied research—survey of the liteiatuie from 2010. J. Mol. Recogn. 25(1), 32-52... 

As it has been already mentioned, isothermal microcalorimeters are those calorimeters designed to work in the microwatt range under essentially isothermal conditions. Isothermal titration microcalorimetry (IT xC) is designed to connect extremely sensitive thermal measurement equipment (approx. 20-100 nanowatts) with an automatic syringe able to add reactants in successive injections to the solution with a precision of few nanoliters [32, 33]. Each injection produces specific heat effect, as shown in Fig. 10.5. The determination of heats evolved as a result of interaction between molecules is a main application of this variation of calorimetry. Consequently, isothermal titration calorimetry is a suitable method for studying degradations and biodegradations of versatile pollutants. 

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