Current Drug Targets

Francis J. Castellino
Kleiderer-Pezold Professor of Biochemistry
Director, W.M. Keck Center for Transgene Research
Dean Emeritus, College of Science
230 Raclin-Carmichael Hall, University of Notre Dame
Notre Dame, IN 46556
USA

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Experimental Approaches to Evaluate the Thermodynamics of Protein- Drug Interactions

Author(s): Walter Filgueira de Azevedo Jr. and Raquel Dias

Affiliation: Av. Ipiranga, 6681, CEP 90619-900, Porto Alegre, Rio Grande do Sul, Brazil.

Abstract:

Precise experimental methods to determine ligand-binding affinity are needed to accelerate the discovery of new drugs. Assessing protein-ligand interaction is of great importance for drug development. One of the techniques that may be used to evaluate ligand-binding affinitty is isothermal titration calorimetry (ITC). This experimental methodology may be used to measure the heat of binding of a ligand to a protein. Furthermore, the development of new empirical scoring functions to assess evaluation protein-ligand interaction lack abundance of experimental information to be used to generate reliable scores. ITC technique may be used to fill this gap. Here we describe the application of this technique to ligand-binding affinity determination, and discuss the synergetic relationship between ITC data and the development of a new generation of empirical scoring functions.

Keywords: Isothermal titration calorimetry (ITC), virtual screening, protein-drug interaction, empirical scoring function

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Article Details

VOLUME: 9
ISSUE: 12
Page: [1071 - 1076]
Pages: 6
DOI: 10.2174/138945008786949441
Price: $58