The role of the βasp residue in copper(II) binding by modified peptides

Hanna Czapor-Irzabek, Marek Cebrat, Justyna Brasuń

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


The synthesis and binding abilities of peptides containing β-amino acids towards Cu(II) ions are presented. The peptides studied were: Ala-βAsp-Ser-Gly and Arg-Lys-βAsp-Val-Tyr. Potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, CD) in strict correlation with potentiometric measurements. The results obtained on the β-peptides studied allowed the characterization of the influence of this structural modification on the coordination abilities of the peptides. Moreover, the role of the α-Asp position in the peptide chain was also described.

Original languageEnglish (US)
Pages (from-to)1652-1655
Number of pages4
JournalTetrahedron Letters
Issue number13
StatePublished - Mar 28 2012
Externally publishedYes


  • β-Amino acid
  • β-Peptide
  • Complex
  • Copper(II)

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Drug Discovery


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