Bestatin Induces Specific Changes in Trypanosoma cruzi Dipeptide Pool | Zendy

Andrea Trochine | Zendy; Darren J. Creek | Zendy; Paula FaralTello | Zendy; Michael P. Barrett | Zendy; Carlos Robello | Zendy

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Bestatin Induces Specific Changes in Trypanosoma cruzi Dipeptide Pool

Author(s) -

Andrea Trochine,

Darren J. Creek,

Paula FaralTello,

Michael P. Barrett,

Carlos Robello

Publication year - 2015

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.05046-14

Subject(s) - trypanosoma cruzi , dipeptide , proteases , aminopeptidase , biochemistry , biology , microbiology and biotechnology , chagas disease , leucine , enzyme , chemistry , peptide , amino acid , virology , parasite hosting , world wide web , computer science

Proteases and peptidases inTrypanosoma cruzi are considered potential targets for antichagasic chemotherapy. We monitored changes in low-mass metabolites inT. cruzi epimastigotes treated with bestatin, a dipeptide metalloaminopeptidase inhibitor. After treatment, multiple dipeptides were shown to be increased, confirmingin situ inhibition of the leucine aminopeptidase ofT. cruzi (LAPTc) and probably other peptidases.

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