A new chapter in CK2 targeting : bivalent precision, deep tumor impact
CK2 is a master regulator of survival and resistance pathways across a wide range of cancers - including pediatric and orphan indications. Its clinical relevance is well supported by decades of research.
With our lead asset, we are advancing a bivalent small molecule inhibitor that engages both the ATP-binding pocket and a neighboring allosteric site on the CK2α subunit. This dual-site binding enhances selectivity, sustains inhibition, and blocks both catalytic activity and non-catalytic pro-survival functions of CK2.
Unlike first-generation CK2 inhibitors, our approach was specifically designed to overcome historical limitations - driving selective cancer cell death through a differentiated, validated mechanism with the potential for durable clinical impact.
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Selectivity
Our bivalent inhibitor engages a cryptic allosteric pocket conserved within CK2 but divergent across the broader kinome - enabling high selectivity and reduced off-target effects.
Cancer persistence
Our bivalent binding strategy enables prolonged CK2 engagement and functional blockade, aiming to disrupt mechanisms of tumor adaptability and persistence - key contributors to relapse in difficult-to-treat cancers.
Broader functional modulation
Beyond catalytic inhibition, allosteric site engagement may interfere with CK2’s pro-survival functions that are not addressed by classical ATP-competitive inhibitors - offering a broader therapeutic effect.
Tumor-selective cell death
Unlike pan-kinase inhibitors, our compound has demonstrated preferential cytotoxicity in tumor cells over healthy cells in preclinical models - supporting the potential for reduced systemic toxicity and broader therapeutic windows.