Kinetics and docking studies of two potential new inhibitors of the nucleoside hydrolase from Leishmania donovani

In this study the recombinant enzyme nucleoside hydrolase of Leishmania donovani was expressed in Escherichia coli in connection with maltose binding protein

Magdalena Nascimento Rennó

2012

Scholarcy highlights

  • In this study the recombinant enzyme nucleoside hydrolase of Leishmania donovani was expressed in Escherichia coli in connection with maltose binding protein
  • From the coupled reaction with xanthine oxidase it was possible to determine the kinetic constants of rLdNH–MBP as KM and Vmax
  • Two nucleoside analogs were tested as prototypes of rLdNH inhibitors. These compounds presented high affinity for the enzyme with Ki values of 1.6 ± 0.2 and 17.0 ± 2.1 μM, respectively, as well as 271 and 26 folds higher than the affinity constant found for inosine
  • Additional docking studies showed the binding manner of compounds 1 and 2 inside the active site of LdNH revealing the essential residues for an effective inhibition
  • These results confirm that compounds 1 and 2 are strong rLdNH–maltose binding protein inhibitors

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