Selective ruthenium labeling of the tryptophan residue in the bee venom Peptide melittin

Chemistry. 2015 Mar 23;21(13):4923-5. doi: 10.1002/chem.201406510. Epub 2015 Feb 16.


Melittin is a membrane-active peptide from bee venom with promising antimicrobial and anticancer activity. Herein we report on a simple and selective method for labeling of the tryptophan residue in melittin by the organometallic fragment [(C5 H5 )Ru](+) in aqueous solution and in air. Ruthenium coordination does not disturb the secondary structure of the peptide (as verified by 2D NMR spectroscopy), but changes the pattern of its intermolecular interactions resulting in an 11-fold decrease of hemolytic activity. The high stability of the organometallic conjugate allowed the establishment of the biodistribution of the labeled melittin in mice by inductively coupled plasma MS analysis of ruthenium.

Keywords: bioorganometallic chemistry; melittin; peptide labeling; ruthenium; sandwich complexes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bee Venoms / chemistry*
  • Melitten / chemistry*
  • Mice
  • Molecular Sequence Data
  • Molecular Structure
  • Peptides
  • Ruthenium / chemistry*
  • Tryptophan / chemistry*


  • Bee Venoms
  • Peptides
  • Melitten
  • Ruthenium
  • Tryptophan