Litcius/Paper detail

The Discovery of RP-2119: A Potent, Selective, and Orally Bioavailable Polθ ATPase Inhibitor

Philippe Mochirian, Robert Papp, Marie‐Claude Mathieu, Gino B. Ferraro, Evelyne Dietrich, Bingcan Liu, David Bendahan, Alexander L. Perryman, Simon Surprenant, Sara Fournier, Bita Lotfollahzadeh Barzili, Alexanne Bonneau-Fortin, Shou Yun Yin, Marie-Ève Leclaire, Charmi Patel, Hugo Poirier, Sai Save, Yann Mathieu, Nicolas Morin, Claude Godbout, Helen E. Burston, Karl E. Zahn, Mohamed Adel Attia, Thomas Pinter, Francis Barabé, Paranjay Parikh, Chandresh Jagani, Gyunghoon Kang, Giovanna Scapin, Yaël Mamane, Agnel Sfeir, P. Mäder, Frank Sicheri, Michal Zimmermann, Anne Roulston, Stephen J. Morris, W. Cameron Black, Michel Gallant

2025Journal of Medicinal Chemistry8 citationsDOI

Abstract

DNA polymerase theta (Polθ) plays a critical role in repairing DNA double-strand breaks through microhomology-mediated end joining (MMEJ) and has emerged as a key synthetic lethal drug target in cancers with homologous recombination (HR) deficiencies. Its inhibition has shown a strong potential to synergize with PARP inhibitors, particularly in tumors with deleterious BRCA1 or BRCA2 mutations. Here, we describe the discovery and preclinical development of RP-2119, a selective, potent, and bioavailable Polθ ATPase inhibitor. Starting from a high-throughput ATPase screen combined with literature insights, key vectors for enhancing potency were identified by structural studies using single-particle cryo-electron microscopy (cryo-EM) that revealed the inhibitor binding site. Further optimization of potency and ADME properties led to the identification of RP-2119 with robust in vitro cellular activity in a wide range of HR-deficient cancer cell lines. In HR-deficient cell line- and patient-derived mouse xenografts, RP-2119 demonstrated strong synergy with the PARP inhibitor, olaparib, without exacerbating its hematological toxicity.

Topics & Concepts

ChemistryADMEDrug discoveryPotencyBiochemistryHomologous recombinationATPasePARP inhibitorDNAPharmacologyIn vitroDNA repairDNA damageBioavailabilityIn vivoPolymeraseEnzyme inhibitorPoly ADP ribose polymeraseDrugEnzymeCellOligonucleotideMechanism of actionCell growthStructure–activity relationshipHomologous chromosomeBiological activityCell cultureDrug developmentIn vitro toxicologyCancerCancer cellLead compoundDNA Repair MechanismsPARP inhibition in cancer therapyCancer therapeutics and mechanisms