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Related Experiment Video

Updated: Jul 7, 2026

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
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Copper(II) ion binding to cellular prion protein.

Jernej Zidar1, Elizabeta T Pirc, Milan Hodoscek

  • 1National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia. zidar@cmm.ki.si

Journal of Chemical Information and Modeling
|February 6, 2008
PubMed
Summary

Researchers investigated copper(II) ion binding in cellular prion protein, crucial for understanding prion diseases. Findings indicate copper(II) binds to His 187, not other sites, offering insights into neurodegenerative disease mechanisms.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Prion diseases are fatal neurodegenerative disorders.
  • These diseases are linked to the conversion of normal cellular prion protein (PrP^C) to a pathogenic scrapie isoform (PrP^Sc).
  • Copper(II) ions are experimentally implicated in this conversion process.

Purpose of the Study:

  • To identify and evaluate potential copper(II) ion binding sites in the C-terminal region of PrP^C.
  • To elucidate the role of copper(II) in prion protein's structural changes.

Main Methods:

  • Utilized an ab initio Quantum Mechanics/Molecular Mechanics (QM/MM) computational approach.
  • Integrated computational findings with existing experimental data.
  • Focused on the C-terminal portion of the cellular prion protein.

Main Results:

  • Identified three potential copper(II) ion binding sites within the C-terminal region of PrP^C.
  • Computational and experimental data suggest copper(II) preferentially binds to Histidine 187 (His 187).
  • Binding to Histidine 140 (His 140) and Histidine 177 (His 177) was not supported by the study.

Conclusions:

  • Copper(II) ion binding to His 187 is a key interaction in the cellular prion protein.
  • This specific binding may play a significant role in the initial stages of prion protein misfolding.
  • Understanding copper(II)-PrP^C interactions offers potential therapeutic targets for prion diseases.