Identification of Vimentin Binding to the Derivative of Saurolactam with Antiresorptive Activity by Using Its Chemical Affinity Probe

In the application of proteomics, the entire complement of expressed proteins (the proteome) can be presented in terms of their regulation by multiple factors including cytokines, metabolites, and chemicals or as they are expressed in distinct cellular processes, whereas chemical proteomics involves the identification and validation of the target protein(s) of a parti- cular bioactive small molecule. Thus, correlation of a property or mechanism of the chemical with a specific biological process and, further, the discovery of new target proteins that bind to a class of chemicals or drugs with good efficacy could be starting points for the development of new therapeutics for diseases by using the screening systems based on the structure of the newly identified target protein. 1 The process to identify and validate the protein targets of bioactive small molecules discovered through cell-based assays is an important step in preclinical drug development. Several strategies have been developed to detect target protein(s) that can directly interact with the bioactive small molecule. For the specific capture of target proteins and the rapid mapping of pep- tides containing binding-epitopes, ligand-encapsulated nano- probes and photoaffinity probes have been used in several studies; some of these probes are able to distinguish the inter- actions between the small molecule and its target protein even though the binding interactions are weak and readily reversible. 2