An in vitro study of interactions between insulin-mimetic zinc(II) complexes and selected plasma components

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Abstract

The speciations of some potent insulin-mimetic zinc(II) complexes of bidentate ligands: maltol and 1,2-dimethyl-3-hydroxypyridinone with (O,O) and picolinic acid with (N,O) coordination modes, were studied via solution equilibrium investigations of the ternary complex formation in the presence of small relevant bioligands of the blood serum such as cysteine, histidine and citric acid. Results show that formation of the ternary complexes, especially with cysteine, is favoured at physiological pH range in almost all systems studied. Besides these low molecular mass binders, serum proteins among others albumin and transferrin can bind zinc(II) or its complexes. Accordingly, the distribution of zinc(II) between the small and high molecular mass fractions of the serum was also studied by ultrafiltration. Modelling calculations relating to the distribution of zinc(II), using the stability constants of the ternary complexes studied and those of the serum proteins reported in the literature, confirmed the ultrafiltration results, namely, the primary role of albumin in zinc(II) binding among the low and high molecular mass components of the serum.

Original languageEnglish
Pages (from-to)1936-1945
Number of pages10
JournalJournal of Inorganic Biochemistry
Volume100
Issue number12
DOIs
Publication statusPublished - Dec 2006

Fingerprint

Zinc
Insulin
Plasmas
Molecular mass
Ultrafiltration
Cysteine
Blood Proteins
Albumins
Serum
Transferrin
Histidine
Citric Acid
Binders
Blood
In Vitro Techniques
Ligands

Keywords

  • Insulin-mimetic zinc(II) complexes
  • Solution equilibrium study
  • Ternary complexes
  • Ultrafiltration

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

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title = "An in vitro study of interactions between insulin-mimetic zinc(II) complexes and selected plasma components",
abstract = "The speciations of some potent insulin-mimetic zinc(II) complexes of bidentate ligands: maltol and 1,2-dimethyl-3-hydroxypyridinone with (O,O) and picolinic acid with (N,O) coordination modes, were studied via solution equilibrium investigations of the ternary complex formation in the presence of small relevant bioligands of the blood serum such as cysteine, histidine and citric acid. Results show that formation of the ternary complexes, especially with cysteine, is favoured at physiological pH range in almost all systems studied. Besides these low molecular mass binders, serum proteins among others albumin and transferrin can bind zinc(II) or its complexes. Accordingly, the distribution of zinc(II) between the small and high molecular mass fractions of the serum was also studied by ultrafiltration. Modelling calculations relating to the distribution of zinc(II), using the stability constants of the ternary complexes studied and those of the serum proteins reported in the literature, confirmed the ultrafiltration results, namely, the primary role of albumin in zinc(II) binding among the low and high molecular mass components of the serum.",
keywords = "Insulin-mimetic zinc(II) complexes, Solution equilibrium study, Ternary complexes, Ultrafiltration",
author = "E. Enyedy and L{\'a}szl{\'o} Horv{\'a}th and K. Gajda-Schrantz and G. Galb{\'a}cs and T. Kiss",
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T1 - An in vitro study of interactions between insulin-mimetic zinc(II) complexes and selected plasma components

AU - Enyedy, E.

AU - Horváth, László

AU - Gajda-Schrantz, K.

AU - Galbács, G.

AU - Kiss, T.

PY - 2006/12

Y1 - 2006/12

N2 - The speciations of some potent insulin-mimetic zinc(II) complexes of bidentate ligands: maltol and 1,2-dimethyl-3-hydroxypyridinone with (O,O) and picolinic acid with (N,O) coordination modes, were studied via solution equilibrium investigations of the ternary complex formation in the presence of small relevant bioligands of the blood serum such as cysteine, histidine and citric acid. Results show that formation of the ternary complexes, especially with cysteine, is favoured at physiological pH range in almost all systems studied. Besides these low molecular mass binders, serum proteins among others albumin and transferrin can bind zinc(II) or its complexes. Accordingly, the distribution of zinc(II) between the small and high molecular mass fractions of the serum was also studied by ultrafiltration. Modelling calculations relating to the distribution of zinc(II), using the stability constants of the ternary complexes studied and those of the serum proteins reported in the literature, confirmed the ultrafiltration results, namely, the primary role of albumin in zinc(II) binding among the low and high molecular mass components of the serum.

AB - The speciations of some potent insulin-mimetic zinc(II) complexes of bidentate ligands: maltol and 1,2-dimethyl-3-hydroxypyridinone with (O,O) and picolinic acid with (N,O) coordination modes, were studied via solution equilibrium investigations of the ternary complex formation in the presence of small relevant bioligands of the blood serum such as cysteine, histidine and citric acid. Results show that formation of the ternary complexes, especially with cysteine, is favoured at physiological pH range in almost all systems studied. Besides these low molecular mass binders, serum proteins among others albumin and transferrin can bind zinc(II) or its complexes. Accordingly, the distribution of zinc(II) between the small and high molecular mass fractions of the serum was also studied by ultrafiltration. Modelling calculations relating to the distribution of zinc(II), using the stability constants of the ternary complexes studied and those of the serum proteins reported in the literature, confirmed the ultrafiltration results, namely, the primary role of albumin in zinc(II) binding among the low and high molecular mass components of the serum.

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KW - Solution equilibrium study

KW - Ternary complexes

KW - Ultrafiltration

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