200354-59-2Relevant academic research and scientific papers
Benzoxazin-4-ones as novel, easily accessible inhibitors for rhomboid proteases
Yang, Jian,Barniol-Xicota, Marta,Nguyen, Minh T.N.,Ticha, Anezka,Strisovsky, Kvido,Verhelst, Steven H.L.
, p. 1423 - 1427 (2018)
Rhomboid proteases form one of the most widespread intramembrane protease families. They have been implicated in variety of human diseases. The currently reported rhomboid inhibitors display some selectivity, but their construction involves multistep synthesis protocols. Here, we report benzoxazin-4-ones as novel inhibitors of rhomboid proteases with a covalent, but slow reversible inhibition mechanism. Benzoxazin-4-ones can be synthesized from anthranilic acid derivatives in a one-step synthesis, making them easily accessible. We demonstrate that an alkoxy substituent at the 2-position is crucial for potency and results in low micromolar inhibitors of rhomboid proteases. Hence, we expect that these compounds will allow rapid synthesis and optimization of inhibitors of rhomboids from different organisms.
Studies on 2-benzyloxy-4H-3,1-benzoxazin-4-ones as serine protease inhibitors
Guetschow, Michael,Neumann, Ulf,Sieler, Joachim,Eger, Kurt
, p. 95 - 103 (2007/10/03)
The class of 3,1-benzoxazin-4-ones includes potent inhibitors of various serine proteases. Structural investigations on three 2-benyloxy-4H-3,1-benzoxazin-4-ones (1-3) are described with respect to their reactivity to alkaline hydrolysis. The 13/sup
Inhibition of cathepsin G by 4H-3,1-benzoxazin-4-ones
Guetschow, Michael,Neumann, Uf
, p. 1935 - 1942 (2007/10/03)
A series of 4H-3,1-benzoxazin-4-ones is reported that inhibit the serine proteases human cathepsin G and bovine chymotrypsin. The synthesis and kinetic parameters of the alkaline hydrolysis is described. These compounds act as acyl-enzyme inhibitors of bo
