Inhibition of protein-protein interactions with low molecular weight compounds
Marilyn M Matthews1, David J Weber, Paul S Shapiro
1Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, 20 Penn Street, Baltimore, MD, 21201.
Abstract:
An overview of issues associated with the design and development of low molecular weight inhibitors of protein-protein interactions is presented. Areas discussed include information on the nature of protein-protein interfaces, methods to characterize those interfaces and methods by which that information is applied towards ligand identification and design. Specific examples of the strategy for the identification of inhibitors of protein-protein interactions involving the proteins p56lck kinase, ERK2 and the calcium-binding protein S100B are presented. Physical characterization of the inhibitors identified in those studies shows them to have drug-like and lead-like properties, indicating their potential to be developed into therapeutic agents.
Related Concept Videos
Protein-protein Interfaces
Enzyme Inhibition
Protein-Drug Binding: Mechanism and Kinetics
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Factors Affecting Protein-Drug Binding: Drug Interactions
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Inhibitors of Viral Protein Synthesis
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

