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γ-Secretase inhibitors and modulators act on the intramembrane protease that cleaves amyloid precursor protein (APP). The enzyme is a multiprotein complex with presenilin as its catalytic subunit, and Notch receptors are among its substrates. In 1998, loss of presenilin-1 in neurons was shown to block the γ-secretase cleavage of APP that releases amyloid-β (Aβ). A year later, a presenilin-1-dependent protease was found to release the Notch intracellular domain. DAPT, LY-411575 and semagacestat inhibit both APP and Notch processing and are used in Aβ and Notch signaling studies. Avagacestat and RO4929097 are further inhibitors, and DAPT is also common in organoid and stem cell work. E 2012 is a γ-secretase modulator that shifts Aβ production.
