Targeting protein/protein interactions in drug design
Protein/Protein interactions define a large fraction of the validated targets for drug development including cancer, inflammation, diabetes, osteoporosis, infection and autoimmune diseases.
Until now Protein/Protein interactions have been disrupted or replaced by other proteins. For example, antibodies or chimeric constructs are used to inhibit ligand/receptor interactions, and recombinant proteins are used as substitutes for deficient or insufficient natural proteins. The use of small molecules as antagonists or agonists of protein/protein interactions is still in its early days. The successful targeting of protein/protein interactions requires a precise characterization of the protein partners, their interaction and the allosteric consequences of that interaction. As illustrated in this chapter, Microcalorimetry is ideally suited to perform this characterization.
Introduction
Protein/Protein interactions define a large fraction of the validated targets for drug development including cancer, inflammation, diabetes, osteoporosis, infection and autoimmune diseases. Until now Protein/Protein interactions have been disrupted or replaced by other proteins. For example, antibodies or chimeric constructs are used to inhibit ligand/receptor interactions, and recombinant proteins are used as substitutes for deficient or insufficient natural proteins. The use of small molecules as antagonists or agonists of protein/protein interactions is still in its early days. The successful targeting of protein/protein interactions requires a precise characterization of the protein partners, their interaction and the allosteric consequences of that interaction. As illustrated in this chapter, Microcalorimetry is ideally suited to perform this characterization.
