Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design.
The binding of two biomolecules viewed from the atomic level is highly complex. It involves the formation or removal of many individual non-covalent bonds both between the interacting molecules as well as with solvent. Currently, our understanding of the thermodynamic quantification of biomolecular interactions is somewhat naïve. ITC (isothermal titration calorimetry) provides a rapid route to a full thermodynamic characterization of a biomolecular interaction. Armed with these data, what are we really able to understand about complex formation and can any of this information provide a useful tool to aid drug development? Correlations between thermodynamic data and structural detail have been investigated, allowing insight into ways in which these can be used to understand protein-ligand interactions and provide input into the decision-making process in drug development.
Ladbury
John E
JE
Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Unit 1000, 1515 Holcombe Boulevard, Houston, TX 77030, USA. jeladbury@mdanderson.org
D000818:Animals; D002151:Calorimetry / Q000379:methods* / Q000706:statistics & numerical data*; D032882:Comprehension; D015195:Drug Design; D004347:Drug Interactions; D006801:Humans; D008024:Ligands; D046911:Macromolecular Substances / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods; D013816:Thermodynamics
D008024:Ligands; D046911:Macromolecular Substances