ATP-dependent IFN- α is designed to avoid the systemic toxicity associated with recombinant IFN- α therapy. While in circulation, the therapeutic remains in an inactive conformation. Upon binding to extracellular ATP in the tumor microenvironment, ATP-dependent IFN- α undergoes a conformational change, and the IFN- α component becomes accessible to its cell surface receptor. IFN- […]

ATP-dependent IL-12 is engineered to remain inactive in circulation to avoid the systemic toxicity associated with recombinant IL-12 therapy. Following binding to extracellular ATP present in the tumor, ATP-dependent IL-12 undergoes a conformational change, and the active IL-12 component becomes accessible to IL-12R. IL-12 signaling then drives anti-cancer immunity through effector immune cell differentiation and […]

LAG-3 dependent IL-2 is designed to direct IL-2 activity to tumor-reactive T cells. LAG-3 is absent on the majority of T cells in circulation. Directing IL-2 activity specifically to LAG-3+ T cells has the potential to stimulate the anti-tumor T cell response while minimizing systemic toxicity. Preclinical Development of cLAG3-IL2 commenced Q3 2024.

LRRC15-dependent IFN-⍺ is designed to avoid the systemic toxicity associated with recombinant IFN-⍺ therapy. LRRC15 is highly expressed on suppressive cancer-associated fibroblasts (CAFs). Upon binding to LRRC15, LRRC15-dependent IFN-⍺ undergoes a conformational change, and the IFN-⍺ component becomes accessible to receptor binding in the tumor microenvironment.

LRRC15-dependent anti-TGFβR2 is designed to be inactive in circulation and avoid systemic TGF-β inhibition. LRRC15 is highly expressed on suppressive cancer-associated fibroblasts (CAFs). Upon binding to LRRC15, the therapeutic undergoes a conformational change to reveal the anti-TGFβR2 component, which will block TGFβR2. Inhibition of TGF-β signaling in LRRC15-expressing CAFs reverses their immunosuppressive phenotype, reduces tumor […]

PD-1-dependent IL-12 is designed to circulate in an inactive form, thereby reducing IL-12-driven toxicity. Upon binding to PD-1 on a tumor-reactive T cell, PD-1-dependent IL-12 undergoes a conformational change to reveal active IL-12. In addition to selectively delivering IL-12, PD-1-dependent IL-12 functionally blocks PD-1/PD-L1 signaling.

PD-L1-dependent IFN-α is designed to avoid the systemic toxicity associated with recombinant IFN-α therapy. Upon binding to PD-L1, PD-L1-dependent IFN-α undergoes a conformational change, and the IFN-α component becomes accessible to its cell surface receptor.