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Special Issue "Isothermal Titration Calorimetry"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Physical Chemistry, Theoretical and Computational Chemistry".

Deadline for manuscript submissions: closed (31 May 2009)

Special Issue Editors

Guest Editor
Prof. Dr. Tom L. Blundell

Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, UK
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Guest Editor
Dr. Alan Brown

Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, UK
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Special Issue Information

Dear Colleagues,

Over the past decade Isothermal Titration Calorimetry (ITC) has been one of the fastest developing biophysical techniques, no longer constrained to specialist laboratories. Usage growth can be attributed to its near universality in studying biological macromolecular interactions coupled to its ease of use, adaptability and the quality of information that can be derived from a single titration.

ITC accurately determines the binding constant (K), reaction stoichiometry (n) and the thermodynamic contributions of enthalpy (DH) and entropy (TDS) changes to free energies of binding (DG). The combination of thermodynamic and structural information has dramatically enhanced our understanding of biological interactions in solution.

In this Special Issue, authors describe and analyse some of the most exciting new applications of ITC, including the use of ITC as a practical tool in enzyme assay development, studying small molecule-protein interactions in drug discovery and dissecting thermodynamic cooperativity in multivalent systems. This issue also demonstrates the application range of ITC with reviews describing interactions involving copolymers, surfactants, lipids and nucleic acid G-quadruplexes.

Alan Brown
Tom L. Blundell
Guest Editors

Keywords

  • isothermal titration calorimetry
  • biocalorimetry
  • microcalorimetry
  • thermodynamic parameters of biochemical interactions
  • binding affinity, enthalpy changes and binding stoichiometry measurements
  • Gibbs energy
  • entropy change

Published Papers (8 papers)

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Research

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Open AccessArticle On the Physical Meaning of the Isothermal Titration Calorimetry Measurements in Calorimeters with Full Cells
Int. J. Mol. Sci. 2009, 10(12), 5296-5325; doi:10.3390/ijms10125296
Received: 7 October 2009 / Revised: 6 November 2009 / Accepted: 8 December 2009 / Published: 9 December 2009
Cited by 9 | PDF Full-text (188 KB) | HTML Full-text | XML Full-text
Abstract
We have performed a detailed study of the thermodynamics of the titration Process in an isothermal titration calorimeter with full cells. We show that the relationship between the enthalpy and the heat measured is better described in terms of the equation ΔH =
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We have performed a detailed study of the thermodynamics of the titration Process in an isothermal titration calorimeter with full cells. We show that the relationship between the enthalpy and the heat measured is better described in terms of the equation ΔH = Winj + Q (where Winj is the work necessary to carry out the titration) than in terms of ΔH = Q. Moreover, we show that the heat of interaction between two components is related to the partial enthalpy of interaction at infinite dilution of the titrant component, as well as to its partial volume of interaction at infinite dilution. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)
Figures

Open AccessArticle Heats of Mixing Using an Isothermal Titration Calorimeter: Associated Thermal Effects
Int. J. Mol. Sci. 2009, 10(7), 2911-2920; doi:10.3390/ijms10072911
Received: 5 May 2009 / Revised: 10 June 2009 / Accepted: 19 June 2009 / Published: 29 June 2009
Cited by 4 | PDF Full-text (193 KB) | HTML Full-text | XML Full-text
Abstract
The correct determination of the energy generated or absorbed in the sample cell of an Isothermal Titration Calorimeter (ITC) requires a thorough analysis of the calorimetric signal. This means the identification and quantification of any thermal effect inherent to the working method. In
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The correct determination of the energy generated or absorbed in the sample cell of an Isothermal Titration Calorimeter (ITC) requires a thorough analysis of the calorimetric signal. This means the identification and quantification of any thermal effect inherent to the working method. In this work, it is carried out a review on several thermal effects, studied by us in previous work, and which appear when an ITC is used for measuring the heats of mixing of liquids in a continuous mode. These effects are due to: (i) the difference between the temperature of the injected liquid and the temperature of the mixture during the mixing process, (ii) the increase of the liquid volume located in the mixing cell and (iii) the stirring velocity. Besides, methods for the identification and quantification of the mentioned effects are suggested. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)
Open AccessArticle Titration Calorimetry Standards and the Precision of Isothermal Titration Calorimetry Data
Int. J. Mol. Sci. 2009, 10(6), 2752-2762; doi:10.3390/ijms10062752
Received: 19 May 2009 / Revised: 1 June 2009 / Accepted: 15 June 2009 / Published: 18 June 2009
Cited by 36 | PDF Full-text (210 KB) | HTML Full-text | XML Full-text
Abstract
Current Isothermal Titration Calorimetry (ITC) data in the literature have relatively high errors in the measured enthalpies of protein-ligand binding reactions. There is a need for universal validation standards for titration calorimeters. Several inorganic salt co-precipitation and buffer protonation reactions have been suggested
[...] Read more.
Current Isothermal Titration Calorimetry (ITC) data in the literature have relatively high errors in the measured enthalpies of protein-ligand binding reactions. There is a need for universal validation standards for titration calorimeters. Several inorganic salt co-precipitation and buffer protonation reactions have been suggested as possible enthalpy standards. The performances of several commercial calorimeters, including the VP-ITC, ITC200, and Nano ITC-III, were validated using these suggested standard reactions. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)
Open AccessArticle Measurement of Nanomolar Dissociation Constants by Titration Calorimetry and Thermal Shift Assay – Radicicol Binding to Hsp90 and Ethoxzolamide Binding to CAII
Int. J. Mol. Sci. 2009, 10(6), 2662-2680; doi:10.3390/ijms10062662
Received: 25 March 2009 / Revised: 30 May 2009 / Accepted: 3 June 2009 / Published: 10 June 2009
Cited by 32 | PDF Full-text (615 KB) | HTML Full-text | XML Full-text
Abstract
The analysis of tight protein-ligand binding reactions by isothermal titration calorimetry (ITC) and thermal shift assay (TSA) is presented. The binding of radicicol to the N-terminal domain of human heat shock protein 90 (Hsp90aN) and the binding of ethoxzolamide to human carbonic
[...] Read more.
The analysis of tight protein-ligand binding reactions by isothermal titration calorimetry (ITC) and thermal shift assay (TSA) is presented. The binding of radicicol to the N-terminal domain of human heat shock protein 90 (Hsp90aN) and the binding of ethoxzolamide to human carbonic anhydrase (hCAII) were too strong to be measured accurately by direct ITC titration and therefore were measured by displacement ITC and by observing the temperature-denaturation transitions of ligand-free and ligand-bound protein. Stabilization of both proteins by their ligands was profound, increasing the melting temperature by more than 10 ºC, depending on ligand concentration. Analysis of the melting temperature dependence on the protein and ligand concentrations yielded dissociation constants equal to 1 nM and 2 nM for Hsp90aN-radicicol and hCAII-ethoxzolamide, respectively. The ligand-free and ligand-bound protein fractions melt separately, and two melting transitions are observed. This phenomenon is especially pronounced when the ligand concentration is equal to about half the protein concentration. The analysis compares ITC and TSA data, accounts for two transitions and yields the ligand binding constant and the parameters of protein stability, including the Gibbs free energy and the enthalpy of unfolding. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)

Review

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Open AccessReview Analysis of Cooperativity by Isothermal Titration Calorimetry
Int. J. Mol. Sci. 2009, 10(8), 3457-3477; doi:10.3390/ijms10083457
Received: 10 June 2009 / Revised: 28 July 2009 / Accepted: 31 July 2009 / Published: 4 August 2009
Cited by 43 | PDF Full-text (2273 KB) | HTML Full-text | XML Full-text
Abstract
Cooperative binding pervades Nature. This review discusses the use of isothermal titration calorimetry (ITC) in the identification and characterisation of cooperativity in biological interactions. ITC has broad scope in the analysis of cooperativity as it determines binding stiochiometries, affinities and thermodynamic parameters, including
[...] Read more.
Cooperative binding pervades Nature. This review discusses the use of isothermal titration calorimetry (ITC) in the identification and characterisation of cooperativity in biological interactions. ITC has broad scope in the analysis of cooperativity as it determines binding stiochiometries, affinities and thermodynamic parameters, including enthalpy and entropy in a single experiment. Examples from the literature are used to demonstrate the applicability of ITC in the characterisation of cooperative systems. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)
Open AccessReview Isothermal Microcalorimetry to Investigate Non Specific Interactions in Biophysical Chemistry
Int. J. Mol. Sci. 2009, 10(8), 3283-3315; doi:10.3390/ijms10083283
Received: 3 June 2009 / Revised: 21 July 2009 / Accepted: 24 July 2009 / Published: 28 July 2009
Cited by 43 | PDF Full-text (340 KB) | HTML Full-text | XML Full-text
Abstract
Isothermal titration microcalorimetry (ITC) is mostly used to investigate the thermodynamics of “specific” host-guest interactions in biology as well as in supramolecular chemistry. The aim of this review is to demonstrate that ITC can also provide useful information about non-specific interactions, like
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Isothermal titration microcalorimetry (ITC) is mostly used to investigate the thermodynamics of “specific” host-guest interactions in biology as well as in supramolecular chemistry. The aim of this review is to demonstrate that ITC can also provide useful information about non-specific interactions, like electrostatic or hydrophobic interactions. More attention will be given in the use of ITC to investigate polyelectrolyte-polyelectrolyte (in particular DNA-polycation), polyelectrolyte-protein as well as protein-lipid interactions. We will emphasize that in most cases these “non specific” interactions, as their definition will indicate, are favoured or even driven by an increase in the entropy of the system. The origin of this entropy increase will be discussed for some particular systems. We will also show that in many cases entropy-enthalpy compensation phenomena occur. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)
Open AccessReview Applications of Isothermal Titration Calorimetry in Biophysical Studies of G-quadruplexes
Int. J. Mol. Sci. 2009, 10(7), 2935-2957; doi:10.3390/ijms10072935
Received: 5 June 2009 / Revised: 29 June 2009 / Accepted: 29 June 2009 / Published: 2 July 2009
Cited by 38 | PDF Full-text (251 KB) | HTML Full-text | XML Full-text
Abstract
G-quadruplexes are higher-order nucleic acids structures formed by G-rich sequences that are stabilized by tetrads of hydrogen-bonded guanine bases. Recently, there has been growing interest in the study of G-quadruplexes because of their possible involvement in many biological processes. Isothermal titration calorimetry (ITC)
[...] Read more.
G-quadruplexes are higher-order nucleic acids structures formed by G-rich sequences that are stabilized by tetrads of hydrogen-bonded guanine bases. Recently, there has been growing interest in the study of G-quadruplexes because of their possible involvement in many biological processes. Isothermal titration calorimetry (ITC) has been proven to be a useful tool to study the energetic aspects of G-quadruplex interactions. Particularly, ITC has been applied many times to determine the thermodynamic properties of drug-quadruplex interactions to screening among various drugs and to address drug design. In the present review, we will focus on the ITC studies of G-quadruplex structures and their interaction with proteins and drugs and the most significant results will be discussed. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)
Open AccessReview Thermodynamics of Surfactants, Block Copolymers and Their Mixtures in Water: The Role of the Isothermal Calorimetry
Int. J. Mol. Sci. 2009, 10(7), 2873-2895; doi:10.3390/ijms10072873
Received: 27 May 2009 / Revised: 19 June 2009 / Accepted: 19 June 2009 / Published: 29 June 2009
Cited by 5 | PDF Full-text (288 KB) | HTML Full-text | XML Full-text
Abstract
The thermodynamics of conventional surfactants, block copolymers and their mixtures in water was described to the light of the enthalpy function. The two methodologies, i.e. the van’t Hoff approach and the isothermal calorimetry, used to determine the enthalpy of micellization of pure surfactants
[...] Read more.
The thermodynamics of conventional surfactants, block copolymers and their mixtures in water was described to the light of the enthalpy function. The two methodologies, i.e. the van’t Hoff approach and the isothermal calorimetry, used to determine the enthalpy of micellization of pure surfactants and block copolymers were described. The van’t Hoff method was critically discussed. The aqueous copolymer+surfactant mixtures were analyzed by means of the isothermal titration calorimetry and the enthalpy of transfer of the copolymer from the water to the aqueous surfactant solutions. Thermodynamic models were presented to show the procedure to extract straightforward molecular insights from the bulk properties. Full article
(This article belongs to the Special Issue Isothermal Titration Calorimetry)

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