tailieunhanh - Báo cáo khoa học: The propeptide of cruzipain ) a potent selective inhibitor of the trypanosomal enzymes cruzipain and brucipain, and of the human enzyme cathepsin F

Papain-like cysteine proteases of pathogenic protozoa play important roles in parasite growth, differentiation and host cell invasion. The main cysteine proteases of Trypanosoma cruzi(cruzipain) and of Trypanosoma brucei (brucipain) are validated targets for the development of new chemothera-pies. | ễFEBS Journal The propeptide of cruzipain - a potent selective inhibitor of the trypanosomal enzymes cruzipain and brucipain and of the human enzyme cathepsin F Flavia C. G. Reis1 Tatiana F. R. Costa1 Traian Sulea2 Alessandra Mezzetti2 Julio Scharfstein1 Dieter Bromme3 Robert Menard2 and Ana Paula C. A. Lima1 1 Institute de Biofisica Carlos Chagas Filho CCS Universidade Federaldo Rio de Janeiro RJ Brazil 2 Biotechnology Research Institute NationalResearch Councilof Canada Montreal Canada 3 Department of Oraland BiologicalSciences University of British Columbia Vancouver Canada Keywords brucipain cathepsin F cruzipain inhibition propeptide Correspondence A. P. C. A. Lima Instituto de Biofisica Carlos Chagas Filho Bloco G Centro de Ciencias da Saude Universidade Federaldo Rio de Janeiro Cidade Universitaria 21949-900 Rio de Janeiro RJ Brazil Fax 55 21 2280 8193 Tel 55 21 2209 6591 E-mail anapaula@ Received 25 September 2006 revised 30 November 2006 accepted 22 December 2006 Papain-like cysteine proteases of pathogenic protozoa play important roles in parasite growth differentiation and host cell invasion. The main cysteine proteases of Trypanosoma cruzi cruzipain and of Trypanosoma brucei brucipain are validated targets for the development of new chemotherapies. These proteases are synthesized as precursors and activated upon removal of the N-terminal prodomain. Here we report potent and selective inhibition of cruzipain and brucipain by the recombinant full-length prodomain of cruzipain. The propeptide did not inhibit human cathepsins S K or B or papain at the tested concentrations and moderately inhibited human cathepsin V. Human cathepsin F was very efficiently inhibited Ki of 32 pm an interesting finding indicating that cruzipain propeptide is able to discriminate cathepsin F from other cathepsin L-like enzymes. Comparative structural modeling and analysis identified the interaction between the P1p-a3p loop of the propeptide and the propeptide-binding

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