2977-51-7Relevant articles and documents
Ethacrynic acid as a lead structure for the development of potent urease inhibitors
Janser, Ingo,Vortolomei, Caitlyn M.,Meka, Ranjith K.,Walsh, Courtney A.,Janser, Romy F.J.
, p. 660 - 664 (2013/08/15)
Ethacrynic acid and a series of its analogues were synthesized and subsequently evaluated for their inhibitory effect on jack bean urease. Ethacrynic acid showed, even at low concentrations, very potent inhibitory activity against the enzyme. For ethacrynic acid, the inhibition potential increased with increasing preincubation time of ethacrynic acid and enzyme, whereas for some other compounds a higher preincubation time lead to a significant reduction of their activity. We could demonstrate that the α,β-unsaturated carbonyl unit of our compounds is mandatory to inhibit the enzyme, possibly due to its ability to bind to cysteine residues in the active site of the jack bean urease.
Synthesis and Evaluation of Non-peptidic Cysteine Protease Inhibitors of P. falciparum Derived from Etacrynic Acid
Dude, Marie-Adrienne,Kaeppler, Ulrich,Herb, Monika,Schiller, Markus,Schulz, Franziska,Vedder, Birgit,Heppner, Saskia,Pradel, Gabriele,Gut, Jiri,Rosenthal, Philip J.,Schirmeister, Tanja,Leippe, Matthias,Gelhaus, Christoph
scheme or table, p. 19 - 35 (2009/09/08)
A series of etacrynic acid derivatives was synthesized and screened for their in vitro activity against Plasmodium falciparum, as well as their activity against recombinantly expressed falcipain-2 and -3. The two most active compounds of the series displayed IC50 values of 9.0 and 18.8 μM against Plasmodia.
