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Amyloid-β Peptide Induces Prion Protein Amyloid Formation: Evidence for Its Widespread Amyloidogenic Effect

Ryo Honda1

  • 1The United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, 1-1 Yanagido, Gifu, 501-1194, Japan.

Angewandte Chemie (International Ed. in English)
|April 13, 2018
PubMed

Insights

Alzheimer's amyloid-beta (Aβ) peptide induces prion protein (PrP) misfolding into amyloid aggregates. This study shows Aβ can cause widespread, nonspecific protein aggregation, potentially worsening neurodegenerative diseases.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Protein Misfolding Diseases

Background:

  • Transmissible spongiform encephalopathy is linked to prion protein (PrP) misfolding into amyloid aggregates.
  • The interaction between PrP and Alzheimer's disease amyloid-beta peptide (Aβ) and its effect on PrP misfolding is not well understood.

Purpose of the Study:

  • To investigate the in vitro effect of Aβ on PrP misfolding.
  • To determine if Aβ's effect on PrP is sequence-specific.
  • To explore Aβ's potential role in general protein aggregation.

Main Methods:

  • In vitro assays to observe Aβ-induced PrP amyloid formation.
  • Systematic mutagenesis of PrP to identify critical sequences for Aβ interaction.
  • Testing Aβ's effect on other unrelated proteins (insulin, lysozyme) to assess amyloidogenic potential.

Main Results:

  • Aβ induces PrP-amyloid formation at submicromolar concentrations.
  • Aβ does not require specific amino acid sequences in PrP for this effect.
  • Aβ induces amyloid fibril formation in unrelated proteins like insulin and lysozyme.

Conclusions:

  • Aβ has a nonspecific amyloidogenic effect, promoting misfolding of various proteins.
  • This mechanism suggests Aβ may contribute to widespread protein aggregation in neurodegenerative diseases.
  • Aβ could exacerbate the pathology of multiple protein misfolding disorders beyond Alzheimer's disease.
Keywords:
aggregationamyloid beta-peptideprionsprotein folding

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