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Amyloid Fibrils

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, normally used to...

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Related Experiment Video

Updated: May 26, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

A modified Stokes-Einstein equation for Aβ aggregation.

Srisairam Achuthan¹, Bong Jae Chung, Preetam Ghosh

¹Department of Mathematical Sciences, Montclair State University, Montclair, NJ 07043, USA.

BMC Bioinformatics

|December 15, 2011

Summary

This summary is machine-generated.

Researchers modified the Stokes-Einstein equation to better model amyloid-beta (Aβ) aggregation in Alzheimer's disease, accounting for viscosity changes and molecular shape for more accurate diffusion measurements.

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Area of Science:

Biophysics
Physical Chemistry
Neuroscience

Background:

Protein aggregates are implicated in amyloid diseases, including Alzheimer's.
Understanding protein aggregation is crucial for disease pathology.
The Stokes-Einstein equation is used to measure aggregate hydrodynamic radii.

Purpose of the Study:

To modify the Stokes-Einstein equation for a more realistic model of amyloid-beta (Aβ) aggregation.
To accommodate solvent viscosity changes due to solute size and shape.
To validate the model in protofibril lateral association reactions.

Main Methods:

A mixture theory approach was used to modify the Stokes-Einstein equation.
Effective viscosity was modeled as a function of molecular volume fractions.
Incorporated protofibril dimensions and shapes beyond simple spheres.

Main Results:

The modified equation includes effective viscosity dependent on molecular volume fractions and shapes.
Diffusion coefficients are now dependent on molecular concentration and shape.
Experimental comparisons show similar trends in diffusion coefficient variations over time.

Conclusions:

The standard Stokes-Einstein equation is insufficient for Aβ42 aggregation temporal variations.
Modified equation includes improved shape factors and viscosities.
The model is applicable to Aβ aggregation and other protein aggregation systems.