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

Justyna Brasuń, Hanna Czapor, Agnieszka Matera-Witkiewicz, Aleksandra Kotynia, Aleksandra Sochacka, Marek Cebrat

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The coordination abilities of tetrapeptides containing β-amino acids towards Cu(ii) ions are presented. The studied tetrapeptides were: Ac-βAlaHisGlyHis, βAlaHisGlyHis, Ac-βAspHisGlyHis, βAspHisGlyHis, Ac-βAspHisGly-dHis and βAspHisGly-dHis. Thorough potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes and the role of free -αCOO- 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.

Original languageEnglish (US)
Pages (from-to)6518-6523
Number of pages6
JournalDalton Transactions
Volume39
Issue number28
DOIs
StatePublished - Jul 28 2010
Externally publishedYes

ASJC Scopus subject areas

  • Inorganic Chemistry
  • General Medicine

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