Potentiometric and spectroscopic studies on the copper(II) complexes of peptide hormones containing disulfide bridges

Péter Danyi, K. Várnagy, I. Sóvágó, István Schön, Daniele Sanna, Giovanni Micera

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Copper(II) complexes of oxytocin, 4-Glu-oxytocin, 5-Asp-oxytocin, and GlyGlyGly-Lys8-vasopressin were studied by potentiometric, EPR, and UV-visible spectroscopic methods. The formation of 4N-coordinated complexes was characteristic of all ligands. This type of coordination is especially favored for oxytocin due to the specific conformation of the ring coupled by the disulfide bridge. The coordination of the γ-carboxylate group of 4-Glu-oxytocin and a disulfide sulfur atom of GlyGlyGly-Lys8-vasopressin was reported to occur in the 2N-complexes over medium pH range.

Original languageEnglish
Pages (from-to)69-78
Number of pages10
JournalJournal of Inorganic Biochemistry
Volume60
Issue number1
DOIs
Publication statusPublished - 1995

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Peptide Hormones
Oxytocin
Vasopressins
Disulfides
Copper
Sulfur
Paramagnetic resonance
Conformations
Ligands
Atoms
Glu(4)-oxytocin
Asp(5)-oxytocin

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Potentiometric and spectroscopic studies on the copper(II) complexes of peptide hormones containing disulfide bridges. / Danyi, Péter; Várnagy, K.; Sóvágó, I.; Schön, István; Sanna, Daniele; Micera, Giovanni.

In: Journal of Inorganic Biochemistry, Vol. 60, No. 1, 1995, p. 69-78.

Research output: Contribution to journalArticle

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AU - Sóvágó, I.

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AU - Sanna, Daniele

AU - Micera, Giovanni

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