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

doi:10.1016/j.ica.2012.09.035

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

Research output: Contribution to journal › Article › peer-review

9 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 language	English (US)
Pages (from-to)	40-48
Number of pages	9
Journal	Inorganica Chimica Acta
Volume	396
DOIs	https://doi.org/10.1016/j.ica.2012.09.035
State	Published - Feb 24 2013
Externally published	Yes

Keywords

Complex
Copper
Histidine
Oxytocin

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry
Materials Chemistry

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10.1016/j.ica.2012.09.035

Cite this

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

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.",

keywords = "Complex, Copper, Histidine, Oxytocin",

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doi = "10.1016/j.ica.2012.09.035",

language = "English (US)",

volume = "396",

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T1 - The role of hydroxyl group of tyrosine in copper(II) binding by His-analogs of oxytocin

AU - Kotynia, Aleksandra

AU - Czyznikowska, Zaneta

AU - Cebrat, Marek

AU - Jaremko, Łukasz

AU - Gładysz, Olimpia

AU - Jaremko, Mariusz

AU - Marciniak, Aleksandra

AU - Brasuń, Justyna

PY - 2013/2/24

Y1 - 2013/2/24

N2 - 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.

AB - 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.

KW - Complex

KW - Copper

KW - Histidine

KW - Oxytocin

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UR - https://www.scopus.com/pages/publications/84875241368#tab=citedBy

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DO - 10.1016/j.ica.2012.09.035

M3 - Article

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SN - 0020-1693

VL - 396

SP - 40

EP - 48

JO - Inorganica Chimica Acta

JF - Inorganica Chimica Acta

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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