#CEITEC MU-001
SUMMARY
The researchers from Masaryk University developed a DNA-aptamer-based inhibitor that, in contrast to FGFR TKIs, inhibits FGFR1 but not the other existing FGFR variants (FGFR2, FGFR3, and FGFR4). In contrast to the current generation of TKIs, which targets the intracellular (kinase) domain of FGFR, the aptamer targets its extracellular domain; it significantly facilitates its potential administration to patients. The nature of the aptamer, being a short oligonucleotide, warrants its high (shelf) stability and low production costs and toxicity. The inhibitor activity and biological stability can be tuned through chemical modifications.
BACKGROUND
Impaired FGFR signalling is associated with many pathological conditions, including growth disorders, degenerative diseases, and cancer. Current therapeutic approaches for targeting FGFR signalling are based on small-molecule inhibitors of FGFR catalytic activity (tyrosine kinase inhibitors, TKIs). However, TKIs lack specificity as they typically inhibit all four existing FGFRs (FGFR1-4) and several unrelated receptor tyrosine kinases, limiting their clinical use due to side effects and toxicity. Fifteen TKIs are currently in clinical trials for tumours caused by lesions in FGFR genes, such as FGFR amplification, activating mutations, and fusion oncogenes involving FGFRs.
FEATURES AND KEY BENEFITS
- Higher specificity – due to the aptamer nature.
- Lower toxicity – as it interacts with the receptor outside the cell.
- New mechanism of action – it impairs the signalling but does not compete with the original FGF ligand.
REFERENCES
Patent application submitted
AVAILABLE
Seeking development partner, commercial partner, licensing, investment.
CONTACT
Lukáš Trantírek, TechTransfer@ceitec.muni.cz
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