Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from Plasmodium falciparum

Research output: Contribution to journalResearch articleContributedpeer-review


  • Komagal K Sivaraman - (Author)
  • Alessandro Paiardini - (Author)
  • Marcin Sieńczyk - (Author)
  • Chiara Ruggeri - (Author)
  • Christine A Oellig - , Monash University (Author)
  • John P Dalton - (Author)
  • Marcin Drag - (Author)
  • Sheena McGowan - (Author)


The malaria parasite Plasmodium falciparum employs two metallo-aminopeptidases, PfA-M1 and PfA-M17, which are essential for parasite survival. Compounds that inhibit the activity of either enzyme represent leads for the development of new antimalarial drugs. Here we report the synthesis and structure-activity relationships of a small library of phosphonic acid arginine mimetics that probe the S1 pocket of both enzymes and map the necessary interactions that would be important for a dual inhibitor.


Original languageEnglish
Pages (from-to)5213-5217
JournalJournal of Medicinal Chemistry
Publication statusPublished - Jun 2013
Externally publishedYes

External IDs

Scopus 84879558016


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