NXP100
(Complement Factor B Inhibitor)
NXP100 is a small molecule for oral, once daily administration that inhibits Factor B, a critical protease within the alternative pathway of the complement cascade. By binding its target, NXP100 halts the formation and stabilization of the alternative pathway’s C3 convertase and its positive feedback amplification loop. This upstream, proximal intervention prevents downstream hyperactivation by stopping the cleavage of C3 into C3b and ultimately blocking the assembly of the C5 convertase and the terminal membrane attack complex. Factor B is a validated target in several complement-mediated diseases, including paroxysmal nocturnal hemoglobinuria (PNH), IgA Nephropathy (IgAN) and C3 Glomerulonephritis (C3G) and is investigated in several others, including Lupus Nephritis (LN), Myasthenia Gravis (MG), and dry Age-Related Macular Degeneration (dAMD).
NXP900
(SRC/YES1 Kinase Inhibitor)
NXP900 is an oral small-molecule inhibitor targeting the SRC Family of Kinases (SFKs), with low nanomolar potency for SRC and YES1.NXP900 functions via a Type 1.5 mechanism, whereby it binds to the kinase in its native, inactive conformation. This structural lock achieves a complete signal shutdown by simultaneously blocking both the catalytic activity and the scaffolding functions that otherwise allow SFK oncogenic signaling, resulting in suppression of cell proliferation, survival, and migration in solid tumors while overcoming bypass resistance mechanisms seen with other targeted therapies.
NXP200
(Paradox Breaker BRAF Inhibitor)
NXP200 is an oral small-molecule, paradox breaker BRAF inhibitor. While first-generation BRAF inhibitors successfully inhibit the oncogenic Class I mutation (BRAFV600), they cause a phenomenon known as paradoxical activation, which results in drug resistance and secondary malignancies. NXP200 circumvents this by physically disrupting the formation of the BRAF dimer, resulting in inhibition of the Class I mutation, and also of the dimerizing, RAS independent (Class II) and RAS-dependent (Class III) mutations.