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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Amyloid Fibrils03:03

Amyloid Fibrils

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Updated: May 22, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Bacterial amyloids.

Yizhou Zhou1, Luz P Blanco, Daniel R Smith

  • 1Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.

Methods in Molecular Biology (Clifton, N.J.)
|April 25, 2012
PubMed
Summary
This summary is machine-generated.

This study details methods for analyzing bacterial amyloids, focusing on curli fibers. These techniques utilize amyloid-specific dyes and biophysical properties for quantification and are applicable to other bacterial amyloid systems.

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Rapid Generation of Amyloid from Native Proteins In vitro
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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Bacteria assemble functional amyloid fibers on their cell surface, often mediating biofilm formation and cell-surface interactions.
  • Bacterial amyloids share structural and biochemical characteristics with disease-associated eukaryotic amyloids.
  • Amyloids' ability to bind dyes like Congo red and resist denaturation aids in their study.

Purpose of the Study:

  • To present basic, broadly applicable methods for studying bacterial amyloids.
  • To focus on the well-characterized curli amyloid fibers from Enterobacteriaceae as a model system.
  • To enable the study of other bacterial amyloids using established amyloid properties.

Main Methods:

  • Utilizing amyloid-specific dyes, such as Congo red, for staining and quantification.
  • Assessing the resistance of bacterial amyloids to denaturation as a key characteristic.
  • Applying biophysical properties inherent to amyloid structures for analysis.

Main Results:

  • Established straightforward methods for scoring and quantifying bacterial amyloid formation.
  • Demonstrated the utility of curli amyloid fibers as a model for studying bacterial amyloids.
  • Validated techniques applicable to diverse bacterial amyloid systems.

Conclusions:

  • The presented methods are accessible and easily implementable in standard molecular biology laboratories.
  • These approaches facilitate the investigation of various bacterial amyloids beyond curli.
  • Understanding bacterial amyloids is crucial for their roles in microbial communities and potential therapeutic targets.