Identification of active Plasmodium falciparum calpain to establish screening system for Pf-calpain-based drug development.

ABSTRACT:

Background

With the increasing resistance of malaria parasites to available drugs, there is an urgent demand to develop new anti-malarial drugs. Calpain inhibitor, ALLN, is proposed to inhibit parasite proliferation by suppressing haemoglobin degradation. This provides Plasmodium calpain as a potential target for drug development. Pf-calpain, a cysteine protease of Plasmodium falciparum, belongs to calpain-7 family, which is an atypical calpain not harboring Ca2+-binding regulatory motifs. In this present study, in order to establish the screening system for Pf-calpain specific inhibitors, the active form of Pf-calpain was first identified.

Methods

Recombinant Pf-calpain including catalytic subdomain IIa (rPfcal-IIa) was heterologously expressed and purified. Enzymatic activ

SUBMITTER: Soh BY 

PROVIDER: S-EPMC3583800 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature