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Aurora kinase inhibitors block Aurora A, Aurora B and Aurora C, three serine/threonine kinases that coordinate mitosis. The founding aurora gene was described in Drosophila in 1995, where its mutations prevented centrosome separation and produced monopolar spindles. In human cells Aurora A acts at centrosomes and spindle poles during spindle assembly. Aurora B belongs to the chromosomal passenger complex, which moves from centromeres to the spindle midzone during division. Alisertib preferentially inhibits Aurora A, whereas barasertib-HQPA and hesperadin mainly target Aurora B. Work with hesperadin in 2003 linked Aurora B to correcting kinetochore-microtubule attachments and maintaining the spindle assembly checkpoint. Tozasertib and AMG 900 inhibit all three family members and are used as pan-Aurora tools.
Aurora A inhibitor 4 (compound C9) is a selective inhibitor of Aurora A kinase, demonstrating a GI50 of 4.26 μM in DU 145 cells and 7.08 μM in HT-29 cells. This compound exhibits significant anti-proliferative effects, making it valuable for research focused on cell cycle regulation and cancer therapeutics. Its ability to inhibit Aurora A activity can be applied in studies investigating mitotic dysregulation in various tumor types.
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Win 47338 is a control compound targeting Aurora kinases (AurA/AurB) and the mitotic kinase monopolar spindle 1 (MPS1). It serves as a crucial reference for studies involving mitotic regulation and cellular division processes. With a Ki value greater than 100 μM, it provides a baseline for evaluating the potency of other kinase inhibitors in research applications focused on cell cycle dynamics and cancer therapeutics.
Aurora B inhibitor 1 is a selective inhibitor of the Aurora B kinase, exhibiting a Ki value of
