2MW6
Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue
Summary for 2MW6
| Entry DOI | 10.2210/pdb2mw6/pdb |
| Related | 2MLT |
| NMR Information | BMRB: 25300 |
| Descriptor | Melittin, [(1,2,3,4,5-eta)-cyclopentadienyl][(1,2,3,4,4a,8a-eta)-naphthalene]ruthenium(1+) (2 entities in total) |
| Functional Keywords | toxin |
| Biological source | Apis mellifera (European honey bee,Western honey bee,bee,honeybee) |
| Total number of polymer chains | 1 |
| Total formula weight | 3144.83 |
| Authors | Perekalin, D.S.,Pavlov, A.A.,Novikov, V.V. (deposition date: 2014-10-28, release date: 2015-07-01, Last modification date: 2024-11-06) |
| Primary citation | Perekalin, D.S.,Novikov, V.V.,Pavlov, A.A.,Ivanov, I.A.,Anisimova, N.Y.,Kopylov, A.N.,Volkov, D.S.,Seregina, I.F.,Bolshov, M.A.,Kudinov, A.R. Selective ruthenium labeling of the tryptophan residue in the bee venom Peptide melittin. Chemistry, 21:4923-4925, 2015 Cited by PubMed Abstract: 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. PubMed: 25688543DOI: 10.1002/chem.201406510 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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