Novel fluorinated pseudopeptides as proteasome inhibitors

We have designed novel small inhibitors of rabbit 20S proteasome using a trifluoromethyl-β-hydrazino acid scaffold. Structural variations influenced their inhibition of the three types of active sites. Proteasome inhibition at the micromolar level was selective, calpain I and cathepsin B were not inhibited.

Graphical abstractA new class of small 20S proteasome inhibitors based on a central trifluoromethyl-β-hydrazino acid scaffold is reported. Proteasome inhibition at the micromolar level was selective, calpain I and cathepsin B were not inhibited.Figure optionsDownload full-size imageDownload as PowerPoint slide