2mw6
Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residueStructure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue
Structural highlights
FunctionMEL_APIME Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.[1] Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.[2] Publication Abstract from PubMedMelittin 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. Selective ruthenium labeling of the tryptophan residue in the bee venom Peptide melittin.,Perekalin DS, Novikov VV, Pavlov AA, Ivanov IA, Anisimova NY, Kopylov AN, Volkov DS, Seregina IF, Bolshov MA, Kudinov AR Chemistry. 2015 Mar 23;21(13):4923-5. doi: 10.1002/chem.201406510. Epub 2015 Feb , 16. PMID:25688543[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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