E-mail a Wiley Online Library Link

Dr. Valentina Aureggi, Veronika Ehmke, Dr. Joerg Wieland, Dr. W. Bernd Schweizer, Dr. Bruno Bernet, Dr. Daniel Bur, Dr. Solange Meyer, Dr. Matthias Rottmann, Céline Freymond, Prof. Dr. Reto Brun, Prof. Dr. Bernhard Breit and Prof. Dr. François Diederich Potent Inhibitors of Malarial Aspartic Proteases, the Plasmepsins, by Hydroformylation of Substituted 7-Azanorbornenes Chemistry - A European Journal 19

Version of Record online: 19 NOV 2012 | DOI: 10.1002/chem.201202941

Thumbnail image of graphical abstract

Pocket change: Hydroformylation is the key step in the synthesis of 7-azanorbornane-based ligands featuring three vectors to occupy the flap, S1/S3, and S1′ subpocket of the malarial aspartic proteases, plasmepsin (PM) I, II, and IV. Occupation of the lipophilic S1′ subpocket leads to high binding potency (IC50 values down to 6 nM) and high selectivity against the related human enzymes hCatD and hCatE. Although the ligands were designed for PM II, the binding to PM IV is particularly enhanced by the newly introduced S1′ substituent.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field