Abstract
Proteins almost never act in an isolated manner; they interact with other proteins in order to perform essential roles in many important cellular processes. Apart from their ability to form stable multiprotein complexes, proteins associate transiently with their targets to modify, regulate by steric effects, or translocate them to different cellular compartments. Therefore, the identification of molecules able to modulate such protein contacts is of significant interest for drug discovery and chemical biology, since it provides a means to exert control over cellular events. Nevertheless, finding antagonists of protein interactions displaying both target affinity and selectivity in the complex context of the cell proteome is a challenging task, because of the generally large, noncontiguous, interfaces involved in protein interactions. In this review we focus on recent advances in the detection, analysis and specific interference of protein interactions. These studies provide the basis for a promising avenue in medicinal chemistry towards the selective regulation of biochemical pathways.
Keywords: Protein-protein interactions, interaction networks, protein arrays, two-hybrid, split reporter complementation, energy transfer techniques, mass spectrometry, drug discovery, bimolecular fluorescence complementation
Related Journals
Current Pharmaceutical Design
Current Topics in Medicinal Chemistry
Current Respiratory Medicine Reviews
Infectious Disorders - Drug Targets
Endocrine, Metabolic & Immune Disorders - Drug Targets
Anti-Infective Agents
Coronaviruses
Recent Advances in Inflammation & Allergy Drug Discovery
Current Probiotics
4