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Related Experiment Videos

Small-molecule aggregates inhibit amyloid polymerization.

Brian Y Feng1, Brandon H Toyama, Holger Wille

  • 1Department of Pharmaceutical Chemistry and Graduate Group in Chemistry and Chemical Biology, University of California San Francisco, 1700 4th Street, San Francisco, California 94158-2330, USA.

Nature Chemical Biology
|January 29, 2008
PubMed
Summary
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Many protein aggregation inhibitors work by forming colloidal aggregates. These aggregates were shown to inhibit amyloid formation in yeast and mouse prion proteins, suggesting a broad biological relevance.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Amyloid inhibitors often share structural similarities with known chemical aggregators.
  • Chemical aggregates are known to inhibit the function of various proteins.
  • Understanding the mechanism of amyloid inhibition is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate whether known chemical aggregators can inhibit amyloid formation.
  • To determine if known anti-amyloid molecules function via colloidal aggregation.
  • To explore the potential biological relevance of colloidal inhibition in amyloid diseases.

Main Methods:

  • Tested eight known chemical aggregators for their effect on yeast (Sup35) and mouse (recMoPrP) prion protein amyloid formation.

Related Experiment Videos

  • Assessed three known anti-amyloid molecules for their effect on beta-lactamase inhibition in a detergent-dependent manner.
  • Utilized electron microscopy to visualize the localization and effect of colloidal aggregates on preformed amyloid fibers.
  • Examined the impact of these inhibitors on yeast cell infection with Sup35 prions.

    • Main Results:

    • Eight chemical aggregators effectively inhibited amyloid formation of Sup35 and recMoPrP, consistent with colloidal inhibition.
    • Three anti-amyloid molecules demonstrated detergent-dependent inhibition of beta-lactamase, suggesting colloidal aggregate formation.
    • Electron microscopy confirmed that colloids localized to preformed fibers and prevented further aggregation.
    • Inhibition of yeast cell infection by Sup35 prions was observed, indicating biological applicability.

    Conclusions:

    • Known chemical aggregators can inhibit prion protein amyloid formation through colloidal inhibition.
    • Anti-amyloid molecules may exert their effects by forming colloidal aggregates.
    • Colloidal inhibition is a potentially significant mechanism relevant to biological systems and prion diseases.