Journal of Biomolecular NMR

, Volume 18, Issue 2, pp 145–151 | Cite as

Production of stable isotope enriched antimicrobial peptides in Escherichia coli: An application to the production of a 15N-enriched fragment of lactoferrin

  • Andreja Majerle
  • Jurka Kidrič
  • Roman Jerala


A method is described for the production of recombinant isotopically enriched peptides in E. coli. Peptides are produced in high yield as fusion proteins with ketosteroid isomerase which form insoluble inclusion bodies. This insoluble form allows easy purification, stabilizes the peptide against degradation and prevents bactericidal activity of the peptide. Cyanogen bromide cleavage released peptide which was conjugated with alkylamines to form lipopeptide. An important advantage of this system is that it allows production of peptides that are toxic to bacteria, which we have demonstrated on a dodecapeptide based on residues 21–31 of human bactericidal protein lactoferrin.

antimicrobial peptide human lactoferrin isotope labeling lipopeptide recombinant peptide 


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Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • Andreja Majerle
    • 1
  • Jurka Kidrič
    • 1
  • Roman Jerala
    • 1
  1. 1.Laboratory for Molecular Modeling and NMR spectroscopyNational Institute of ChemistryLjubljanaSlovenia

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