Towards the targeted protein degradation of CK2: design and synthesis of CAM4066-based PROTACs
Human protein kinase CK2 is a constitutively active serine/threonine kinase implicated in numerous cancers. Although ATP-competitive inhibitors such as CX-4945 show therapeutic potential, they are limited by off-target effects and incomplete or transient CK2 suppression. PROTACs offer an alternative strategy by inducing proteasome-mediated degradation, with potential advantages in potency, selectivity, and duration of action. Herein, a series of CK2-targeting PROTACs has been designed and synthesised. By conjugating a CAM4066-derived warhead to CRBN or VHL ligands, four VHL-recruiting PROTACs, were prepared using PEG and alkyl linkers, alongside two CRBN-recruiting analogues featuring constrained linkers. A ligand–linker analogue in which a linker is projected from the solvent-exposed region of CK2α retained binding affinity comparable to CAM4066, confirming that linker installation is tolerated and preserves key interactions in the αD and ATP sites.
Authors
- Benjamin C. Whitehurst (ORCID: https://orcid.org/0000-0002-5485-1762)
- Marko Hyvönen (ORCID: https://orcid.org/0000-0001-8683-4070)
- Soňa Krajčovičová (ORCID: https://orcid.org/0000-0003-0139-2360)
- P. Brear (ORCID: https://orcid.org/0000-0002-4045-0474)
- David R. Spring (ORCID: https://orcid.org/0000-0001-7355-2824)
- Jason S. Carroll (ORCID: https://orcid.org/0000-0003-3643-0080)
- Sophie Day-Riley (ORCID: https://orcid.org/0009-0003-8558-7217)
- Aryaman Raj Sokhal
- Jan L Venne
Publication Details
- Journal
- Beilstein Journal of Organic Chemistry
- Published
- 2026-04-22
- DOI
- https://doi.org/10.3762/bjoc.22.47
- Primary Topic
- Protein Degradation and Inhibitors
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Diamond Light Source