Domainex is tapping Horizon Discovery for application of the latter’s X-MAN human cell line platform in profiling lead compounds in its TBK1/IKKe oncology R&D program, which is being carried out in collaboration with the U.K.’s Institute of Cancer Research (ICR).
Under terms of the deal Horizon will profile lead TBK1/IKKe dual inhibitor compounds against a panel of X-MAN isogenic disease model cell lines to identify the effects of individual cancer-related gene mutations on drug activity and resistance, in order to help predict which subgroups of patients are most likely to respond to therapy. Domainex says the work will help guide medicinal chemistry optimization and provide patient stratification data that will be valuable for future partnering.
“Horizon’s oncology and genome editing expertise are a valuable complement to our in-house biochemistry, medicinal chemistry and computer-aided drug design capabilities,” comments Eddy Littler, Domainex CEO. “We also look forward to future collaborations with Horizon on Domainex’s epigenetic pipeline in ocology and with the wide number of projects that Domainex supports on behalf of its clients.”
U.K.-based Domainex operates a hybrid business model, offering drug discovery services to external partners, while also developing its own pipeline of anticancer drugs. The firm says TANK-binding kinase 1 (TBK1) and IkappaB kinase epsilon (IKKε) represent validated novel drug targets, with applications in the treatment of cancer, a variety of inflammatory diseases such as rheumatoid arthritis, and obesity. Domainex has identified small molecule inhibitors of TBK1/IKKε and is progressing these as potential therapies for breast and ovarian cancer.
The firm’s drug discovery services span target protein expression, binding assay development, hit identification and integrated medicinal and computational chemistry. The firm’s combinatorial domain hunting (CDH) platform is proprietary technology for quickly identifying soluble, highly expressible constructs of drug target proteins that are able to bind ligand and are suitable for use in structural studies, binding and activity assays. The technology combines a method for the production of unbiased gene-fragment libraries in E. coli, with a screening protocol to provide a comprehensive readout of solubility, ligand binding and yield for thousands of resulting protein fragments.
