Related Experiment Video

Updated: Apr 26, 2026

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
10:03

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

31.2K

A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation

Erwan Hingant1, Pascaline Fontes2, Maria Teresa Alvarez-Martinez3

  • 1CI2MA, Universidad de Concepción, Concepción, Chile.

Plos Computational Biology
|August 8, 2014
PubMed

Insights

This study proposes a new hypothesis for prion amyloid formation, suggesting an intermediate pathway involving micelles to explain in vitro data and mathematical models. It challenges mainstream interpretations of prion protein conformational changes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Mainstream interpretations of prion amyloid formation have faced challenges.
  • Previous work highlighted inconsistencies between in vitro data and mathematical models.
  • A need exists for a unifying hypothesis on prion protein conformational changes.

Purpose of the Study:

  • To propose an original hypothesis for prion amyloid formation.
  • To reconcile in vitro experimental data with mathematical model predictions.
  • To develop a new model for infectious prion amyloidogenesis.

Main Methods:

  • Development of a mathematical model based on a novel hypothesis.
  • Incorporation of hydrodynamic interactions and micelle structures.
  • Comparison of model predictions with experimental data.

Main Results:

  • A proposed intermediate on-pathway for prion protein conformational change.
  • Evidence supporting the role of micelles in forming amyloid-competent isoforms.
  • Alignment of in vitro data with the developed mathematical model.

Conclusions:

  • The proposed hypothesis offers a new perspective on prion protein amyloid formation.
  • Micelles play a crucial role in the conformational transition to amyloidogenic states.
  • The study provides a framework for understanding infectious prion amyloidogenesis.

More Related Videos

Protein Misfolding Cyclic Amplification of Prions10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

18.8K
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

9.4K

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
10.1K
Amyloid Fibrils03:03

Amyloid Fibrils

5.2K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
4.3K