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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 ligand 2 is a selective ligand for the Aurora-A kinase, functioning as a crucial component in PROTAC technology. It plays a significant role in the targeted degradation of Aurora-A, facilitating the investigation of its biological implications in cancer research. This compound is valuable for studying Aurora-A kinases and exploring therapeutic strategies in oncology.
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