Copper(II) complexes of low molecular weight derivatives of thymopoietin

I. Sóvágó, Csilla Bertalan, László Gobi, Imre Sóvágó, Olga Nyéki

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Copper(II) complexes of tri- and tetrapeptides containing either carboxylate or amide group in the side chain were studied by potentiometric and spectroscopic methods. The ligands are tri- and tetrapeptide segments of the hormones thymopoietin and splenin. It was found that internal aspartyl residues significantly enhance the metal binding ability of oligopeptides, resulting in the cooperative deprotonation of the amide nitrogens preceding the aspartyl residue, while the subsequent amide groups do not take part in metal ion coordination. Glutamyl residues have no significant effect on the complex formation processes of oligopeptides.

Original languageEnglish
Pages (from-to)67-75
Number of pages9
JournalJournal of Inorganic Biochemistry
Volume55
Issue number1
DOIs
Publication statusPublished - 1994

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Thymopoietins
Amides
Copper
Oligopeptides
Molecular Weight
Molecular weight
Derivatives
Metals
Deprotonation
Metal ions
Nitrogen
Hormones
Ions
Ligands

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Copper(II) complexes of low molecular weight derivatives of thymopoietin. / Sóvágó, I.; Bertalan, Csilla; Gobi, László; Sóvágó, Imre; Nyéki, Olga.

In: Journal of Inorganic Biochemistry, Vol. 55, No. 1, 1994, p. 67-75.

Research output: Contribution to journalArticle

Sóvágó, I. ; Bertalan, Csilla ; Gobi, László ; Sóvágó, Imre ; Nyéki, Olga. / Copper(II) complexes of low molecular weight derivatives of thymopoietin. In: Journal of Inorganic Biochemistry. 1994 ; Vol. 55, No. 1. pp. 67-75.
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