Replication protein A (RPA) is actually a ssDNA binding protein that's vital for DNA replication and fix. The initiation in the DNA harm selleck screening library response sellectchem by RPA is mediated by protein protein interactions involving the N-terminal domain of the 70 kDa subunit with spouse proteins. Inhibition of these interactions increases sensitivity towards DNA damage and replication anxiety and may perhaps consequently be a potential strategy for cancer drug Tamoxifen discovery. Towards this end, we've discovered two lead series of compounds, derived from hits obtained from a fragment-based display that bind to RPA70N with minimal micromolar affinity and inhibit the binding of an ATRIP-derived peptide to RPA. These compounds may perhaps offer a promising starting up level for that discovery of clinically useful RP inhibitors.