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Purification of Hsp104, a Protein Disaggregase
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Interaction between Hemin and Prion Peptides: Binding, Oxidative Reactivity and Aggregation.

Simone Dell'Acqua1, Elisa Massardi1, Enrico Monzani1

  • 1Dipartimento di Chimica, Università di Pavia, Via Taramelli 12, 27100 Pavia, Italy.

International Journal of Molecular Sciences
|October 17, 2020
PubMed
Summary

Hemin interacts with prion protein (PrP) fragments, with binding affinity increasing with peptide length and histidine content. This interaction may contribute to oxidative stress in neurodegenerative diseases.

Keywords:
heminneurodegenerationoxidative stressperoxidaseprion diseasesprion peptides

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Prion Disease Research

Background:

  • Prion protein (PrP) fragments are implicated in prion diseases and traumatic brain injury.
  • Hemin, an iron-containing porphyrin, is known to interact with various biomolecules.
  • Understanding hemin-PrP interactions may shed light on disease pathogenesis.

Purpose of the Study:

  • To investigate the binding properties of hemin with different prion protein fragments.
  • To assess the potential relevance of these interactions to prion diseases and brain injury.
  • To evaluate the peroxidase-like activity of hemin-PrP complexes.

Main Methods:

  • UV-visible spectrophotometric titration to determine binding constants.
  • Turbidimetry analysis to assess complex solubility and aggregation.
  • Peroxidase activity assays.

Main Results:

  • PrP peptides form a 1:1 adduct with hemin, with binding affinity increasing with peptide length and histidine count.
  • Binding constants (log K1) ranged from 4.80 to 6.48, comparable to hemin-amyloid-β interactions.
  • Hemin induces PrP aggregation, leading to precipitation and preventing further binding constant calculations; peroxidase activity is moderately increased.

Conclusions:

  • Hemin binds to PrP fragments with varying affinities, suggesting a role in modulating PrP behavior.
  • The observed aggregation and increased peroxidase activity of hemin-PrP complexes may contribute to neuronal oxidative stress in neurodegenerative conditions.
  • These findings highlight a potential molecular mechanism linking hemin dysregulation to prion protein-related pathologies.