What is it about?
We provide tridimentional structures for the Trypanosoma cruzi enzymes with trypanothione reductase, cysteine synthase, ATPase, functions, 2,4-dienoyl-CoA reductase, and leishmanolysin activities. The structures were refined by atomistic molecular dynamics (monomer or dimer states) in their in vitro environments (aqueous solution or membrane bilayers) and discussed in the light for drug development.
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Why is it important?
T. cruzi is the protozoan pathogen responsible for Chagas disease, which is a major public health problem in tropical and subtropical regions of developing countries and particularly in Brazil. At moment, there is no therapy available for the prevention (vaccine) and cure (drug) for this disease.
Perspectives
This study open the way for drug design against enzymes specific to T. cruzi that are expected to be essential for this human parasite.
Nicolas Carels
Oswaldo Cruz Foundation
Read the Original
This page is a summary of: In silico structural characterization of protein targets for drug development against Trypanosoma cruzi, Journal of Molecular Modeling, September 2016, Springer Science + Business Media,
DOI: 10.1007/s00894-016-3115-9.
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