Interaction of VIVO, VVO2 and CuII with a peptide analogue SalGly-L-Ala

Tamás Jakusch, Ágnes Dörnyei, Isabel Correia, Lígia M. Rodrigues, Gábor K. Tóth, Tamás Kiss, João Costa Pessoa, Susana Marcão

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The formation of complexes of a tripeptide analogue, salicylglycyl-L-alanine [HOC6H4C(O)NHCH2C(O)NHCH(CH3) -COOH, H2SalGly-L-Ala], was studied with CuII, VIVO and VVO2 in aqueous solution using pH-potentiometric and spectroscopic (UV/Vis, CD, EPR and 51V NMR) techniques. The results demonstrated the ambidentate character of the ligand. The metal ion-induced deprotonation and subsequent coordination of the two neighbouring amide groups was shown to occur in a cooperative way in the pH range 5-6. At pH ≈ 6.5 a complex with an (O-, 2 x CON-, COO-) binding set becomes predominant for both CuII, and VIVO. The affinity of the phenolate-O- for VIVO is high and the ligand is bound to this metal ion even at pH values greater than 10. Conversely, the affinity for VVO2 is significantly lower and no interaction between this metal oxo-ion and the ligand could be detected in the pH range 2-12. In contrast, with the dipeptide analogue H2SalGly, chelation involving the deprotonated amide-N-could be unambiguously detected.

Original languageEnglish
Pages (from-to)2113-2122
Number of pages10
JournalEuropean Journal of Inorganic Chemistry
Issue number11
Publication statusPublished - Jun 2003


  • Bioinorganic chemistry
  • Copper
  • Peptides
  • Speciation
  • Spectroscopy
  • Vanadium

ASJC Scopus subject areas

  • Inorganic Chemistry

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