The unusual coordination abilities of the peptides with betaXaaHisGlyHis sequence. The influence of structural modification of the peptide chain on the copper(II) binding

Dalton Trans. 2010 Jul 28;39(28):6518-23. doi: 10.1039/b923371g. Epub 2010 Jun 11.

Abstract

The coordination abilities of tetrapeptides containing beta-amino acids towards Cu(II) ions are presented. The studied tetrapeptides were: Ac-betaAlaHisGlyHis, betaAlaHisGlyHis, Ac-betaAspHisGlyHis, betaAspHisGlyHis, Ac-betaAspHisGly-dHis and betaAspHisGly-dHis. Thorough potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes and the role of free -alphaCOO(-) side chain group in metal binding. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, EPR, CD) in strict correlation with potentiometric measurements.

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Copper / chemistry*
  • Electron Spin Resonance Spectroscopy
  • Hydrogen-Ion Concentration
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Protein Binding
  • Protein Stability
  • Spectrophotometry, Ultraviolet

Substances

  • Peptides
  • Copper