Probing the dimerization interface of Leishmania infantum trypanothione reductase with site-directed mutagenesis and short peptides

Chembiochem. 2013 Jul 8;14(10):1212-7. doi: 10.1002/cbic.201200744. Epub 2013 Jun 6.

Abstract

Binding at the interface: We tested the inhibitory activity of a set of peptide sequences derived from an α-helix of the dimeric trypanothione reductase from Leishmania infantum. Replacement of a glutamic acid residue with a lysine promoted monomer dissociation and enzyme inhibition.

Keywords: Leishmania; dimer quantification assay; enzyme models; protein-protein interactions; trypanothione reductase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Leishmania infantum / enzymology*
  • Leishmania infantum / genetics
  • Leishmania infantum / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • NADH, NADPH Oxidoreductases / chemistry*
  • NADH, NADPH Oxidoreductases / genetics
  • NADH, NADPH Oxidoreductases / metabolism*
  • Peptides / chemistry*
  • Peptides / genetics
  • Peptides / metabolism*
  • Protein Multimerization

Substances

  • Peptides
  • NADH, NADPH Oxidoreductases
  • trypanothione reductase