Revisiting the antiangiogenic mechanisms of fluorinated thalidomide derivatives

  • Bioorg Med Chem Lett. 2024 Sep 15:110:129858. doi: 10.1016/j.bmcl.2024.129858.
Johannes Sievers  1 Rabea Voget  1 Feiteng Lu  2 Kathleen M Garchitorena  3 Yuen Lam Dora Ng  2 Cindy H Chau  3 Christian Steinebach  1 William D Figg  3 Jan Krönke  2 Michael Gütschow  4
Affiliations
  • 1. Pharmaceutical Institute, Pharmaceutical and Medicinal Chemistry, University of Bonn, An der Immenburg 4, D-53121 Bonn, Germany.
  • 2. Department of Hematology, Oncology, and Cancer Immunology, Charité - Universitätsmedizin Berlin, D-12203 Berlin, Germany.
  • 3. Molecular Pharmacology Section, Genitourinary Malignancies Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
  • 4. Pharmaceutical Institute, Pharmaceutical and Medicinal Chemistry, University of Bonn, An der Immenburg 4, D-53121 Bonn, Germany. Electronic address: [email protected].
Abstract

Introduction of fluorine into bioactive molecules has attracted much attention in drug development. For example, tetrafluorination of the phthalimide moiety of immunomodulatory drugs (IMiDs) has a strong beneficial effect on the ability to inhibit angiogenesis. The neomorphic activity of E3 Ligase complexes is induced by the binding of IMiDs to Cereblon. We investigated that a set of eight thalidomide analogs, comprising non- and tetrafluorinated counterparts, did not induce the degradation of neomorphic substrates (IKZF3, GSPT1, CK1α, SALL4). Hence, the antiangiogenic activity of fluorinated IMiDs was not triggered by neosubstrate degradation features. A fluorine scanning of non-traditional IMiDs of the benzamido glutarimide chemotype was performed. By measuring the endothelial cell tube formation, no angiogenesis inhibitors were identified, confirming the narrow structure-activity window of IMiD-induced antiangiogenesis.

Keywords
Angiogenesis; Cancer therapy; Cereblon; Immunomodulatory drugs; Neosubstrates.