The role of hydroxyl group of tyrosine in copper(II) binding by His-analogs of oxytocin

Aleksandra Kotynia, Zaneta Czyznikowska, Marek Cebrat, Łukasz Jaremko, Olimpia Gładysz, Mariusz Jaremko, Aleksandra Marciniak, Justyna Brasuń*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

In this paper we report on the interaction between the Cu(II) ions and the histidine analogues of oxytocin. The studied His-analogues are characterized by presence of Tyr2 or Phe2 amino acid residues and free or protected N-terminal group. The use of potentiometric methods allowed for the determination of the stoichiometry of formed complexes and calculation of their stability constants. The number of spectroscopic measurements (UV-Vis, CD, NMR, fluorescence) together with the theoretical calculation enabled to obtain the structures of formed complexes and the influence of Tyr2 amino acid residue on the efficiency of metal ion binding.

Original languageEnglish (US)
Pages (from-to)40-48
Number of pages9
JournalInorganica Chimica Acta
Volume396
DOIs
StatePublished - Feb 24 2013
Externally publishedYes

Keywords

  • Complex
  • Copper
  • Histidine
  • Oxytocin

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry
  • Materials Chemistry

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