Cysteine protease falcipain

Double-stranded RNA-mediated gene silencing of cysteine proteases (falcipain-1 and -2) of Plasmodium falciparum. Molecular Microbiology 45, 1245-1254. 

Eksi, S., Czesny, B., Greenbaum, D. C., Bogyo, M., and Williamson, K. C. (2004). Targeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth. Mol. Microbiol. 53, 243-250. 

Sijwali, P. S., and Rosenthal, P. J. (2004). Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum. Proc. 

Li et al. [48] described a virtual screen on the SPECS database to identify inhibitors for the cysteine protease falcipain-2 as promising target for malaria treatment. Based on the available X-ray structure of falcipain-2, two different docking protocols based on Glide [47] and GAsDock [49] were employed to identify 28 nonpeptidic inhibitors. The best compound exhibited an IC50 value of 2.4 pM (Figure 12.2b). Further biochemical evaluations showed that the best inhibitor interacts noncovalently with the active site of this cysteine protease. 

Shenai BR, Sijwali PS, Singh A et al (2000) Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J Biol Chem 275 29000-29010... 

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