Synthesis and Structure-Activity Relationships of Phosphonic Arginine Mimetics as Inhibitors of the M1 and M17 Aminopeptidases from Plasmodium falciparum.
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.
Organizational Affiliation:
Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne, VIC 3800, Australia.
AB [auth E] DA [auth C] DC [auth H] ED [auth K] FA [auth C]
AB [auth E], DA [auth C], DC [auth H], ED [auth K], FA [auth C], FC [auth H], GD [auth K], IB [auth F], KB [auth F], KC [auth I], M [auth A], MA [auth D], MC [auth I], O [auth A], OA [auth D], OD [auth L], QD [auth L], SB [auth G], UB [auth G], UC [auth J], W [auth B], WC [auth J], Y [auth B], YA [auth E]
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