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Copper(II) complexes encapsulated in human red blood cells

R P Bonomo1, A De Flora, E Rizzarelli

  • 1Dipartimento di Scienze Chimiche, Università di Catania, Italy.

Journal of Inorganic Biochemistry
|September 1, 1995
PubMed
Summary

Copper(II) complexes were encapsulated in red blood cells to assess their antioxidant potential. While most complexes remained stable, interactions with hemoglobin and slight oxidative stress were observed, influencing methemoglobin levels.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Materials Science

Background:

  • Copper(II) complexes exhibit labile characteristics, suggesting potential antioxidant properties.
  • Red blood cells (erythrocytes) are a potential delivery vehicle for therapeutic agents.
  • Investigating drug delivery systems requires understanding interactions within the biological environment.

Purpose of the Study:

  • To evaluate the use of copper(II) complexes as antioxidant drugs via encapsulation in human red blood cells.
  • To determine if encapsulation modifies the properties of copper(II) complexes using Electron Spin Resonance (ESR) spectroscopy.
  • To assess the impact of encapsulated copper(II) complexes on erythrocyte metabolic functions and integrity.

Main Methods:

  • Encapsulation of various copper(II) complexes into human red blood cells.

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  • Electron Spin Resonance (ESR) spectroscopy to analyze complex stability and interactions.
  • Assessment of key erythrocyte metabolic parameters: glutathione (GSH), glycolytic rate, hexose monophosphate shunt activity, and Ca(2+)-ATPase.
  • Measurement of methemoglobin levels to evaluate oxidative stress.

    • Main Results:

    • Copper(II) complexes with dipeptides/tripeptides showed interaction with hemoglobin.
    • More stable complexes (copper(II) with TAD or PheANN3) retained their original ESR spectra after encapsulation.
    • Copper(II) complex with GHL induced oxidative stress and complex behavior, including iron(III) species.
    • Encapsulation caused slight oxidative stress in erythrocytes, but major metabolic functions remained largely unaffected.
    • Methemoglobin levels significantly increased with [Cu(GHL)H-1] compared to [Cu(TAD)], indicating complex-dependent hemoglobin interaction.

    Conclusions:

    • Encapsulation of copper(II) complexes in erythrocytes is feasible, but can lead to interactions with hemoglobin and induce mild oxidative stress.
    • The stability and interaction of copper(II) complexes with hemoglobin depend on their specific chemical structure (ligands).
    • Methemoglobin formation is a key indicator sensitive to the type of copper(II) complex encapsulated, highlighting the importance of ligand choice for potential therapeutic applications.