Aph-1c Inhibitors

Chemical inhibitors of aph1 homolog C, a gamma secretase subunit, function by directly interacting with the gamma-secretase complex, resulting in the inhibition of its enzymatic activity. DAPT serves as one such inhibitor, binding to the gamma-secretase complex and consequently reducing the cleavage of its substrate proteins, which includes actions on aph1 homolog C. Similarly, LY-411575 directly targets gamma-secretase, leading to a decrease in the activity of aph1 homolog C in the processing of substrates. Semagacestat and Avagacestat bind to the gamma-secretase complex, thereby inhibiting the function of aph1 homolog C. This inhibition is crucial as it impedes the complex's ability to process amyloid precursor proteins, among others.

Continuing with this theme, Begacestat and PF-3084014 are also known to selectively inhibit gamma-secretase, which diminishes the functional activity of aph1 homolog C within the complex. The precise binding of these inhibitors to the gamma-secretase complex is a pivotal step in the inhibition process, ensuring that aph1 homolog C's role in proteolytic processing is hampered. In addition to these, L-685,458, a transition-state analog inhibitor, and MRK-560, a potent inhibitor, both contribute to the inhibition of aph1 homolog C by hindering the enzymatic activity of the complex. BMS-708163's selective inhibition of gamma-secretase further ensures the direct reduction in the activity of aph1 homolog C. Rounding out the list, Nirogacestat, Elenbecestat, and Atabecestat inhibit gamma-secretase, which in turn leads to a decrease in the functional activity of aph1 homolog C in the enzymatic process of the complex. Each chemical's interaction with the gamma-secretase complex serves to inhibit the function of aph1 homolog C specifically, highlighting the direct relationship between the inhibitor and the targeted protein's activity within the complex.