Discovery and Biological Evaluation of Novel, Potent, and Orally Available CBLB Inhibitors

J Med Chem. 2025 Nov 27;68(22):24502-24518. doi: 10.1021/acs.jmedchem.5c02541. Epub 2025 Nov 12.

Abstract

Casitas B-lineage lymphoma-b (CBLB) has emerged as a promising therapeutic target for cancer immunotherapy due to its central role in modulating T-cell activation and immune tolerance. In this work, we employed a structure-guided drug discovery approach, leveraging the cocrystal structure of CBLB with the hit compound to systematically optimize potency, selectivity, and pharmacokinetic profiles. Through iterative structure-activity relationship (SAR) exploration, we identified compound 10, which is a potent and orally bioavailable CBLB inhibitor with favorable ADME properties. In vivo studies demonstrated that compound 10 exhibits significant antitumor efficacy in syngeneic mouse models, synergizes strongly with anti-PD-1 therapy to enhance tumor regression, and induces durable immune memory against tumor rechallenge. Comprehensive PK/PD analyses revealed sustained target engagement and dose-dependent modulation of downstream biomarkers. Our detailed SAR elucidation provides a roadmap for further optimization of CBLB inhibitors.

MeSH terms

  • Adaptor Proteins, Signal Transducing* / antagonists & inhibitors
  • Adaptor Proteins, Signal Transducing* / metabolism
  • Administration, Oral
  • Animals
  • Antineoplastic Agents* / administration & dosage
  • Antineoplastic Agents* / chemistry
  • Antineoplastic Agents* / pharmacokinetics
  • Antineoplastic Agents* / pharmacology
  • Antineoplastic Agents* / therapeutic use
  • Cell Line, Tumor
  • Drug Discovery*
  • Female
  • Humans
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Proto-Oncogene Proteins c-cbl* / antagonists & inhibitors
  • Proto-Oncogene Proteins c-cbl* / metabolism
  • Structure-Activity Relationship

Substances

  • Proto-Oncogene Proteins c-cbl
  • Adaptor Proteins, Signal Transducing
  • Antineoplastic Agents
  • CBLB protein, human