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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,...

Amyloid Fibrils

Amyloid Fibrils

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Related Experiment Video

Updated: Dec 6, 2025

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Published on: July 6, 2019

Computational Model for Studying Breakage-Dependent Amyloid Growth.

Jennifer Joseph¹, Samir K Maji¹, Ranjith Padinhateeri¹

¹Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400 076, India.

ACS Chemical Neuroscience

|October 14, 2020

Summary

This summary is machine-generated.

This study models amyloid fibril growth kinetics, similar to prion propagation. Simulations reveal how aggregation time and growth rates depend on parameters, aiding early disease detection by quantifying amyloid seeds.

Keywords:

Amyloid filament growth Breaking of amyloid Computational model Growth kinetics Neurodegenerative diseases PMCA Prediction of initial seed concentration

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Last Updated: Dec 6, 2025

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

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Published on: July 6, 2019

Visualizing Axonal Growth Cone Collapse and Early Amyloid β Effects in Cultured Mouse Neurons

Visualizing Axonal Growth Cone Collapse and Early Amyloid β Effects in Cultured Mouse Neurons

Published on: October 30, 2018

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

Area of Science:

Biophysics
Neuroscience
Computational Biology

Background:

Amyloid fibrils are linked to neurodegenerative diseases.
Amyloid proteins can propagate like prions, causing disease spread.
Propagation involves recruiting functional proteins and fibril fragmentation.

Purpose of the Study:

To model the kinetics of amyloid fibril growth via breakage and elongation.
To understand how measurable quantities scale with problem parameters.
To aid in early disease detection by amplifying amyloid seeds.

Main Methods:

Kinetic Monte Carlo simulations.
Mathematical counting methods.
Modeling fibril growth kinetics.

Main Results:

Quantified scaling of 50% aggregation time (T50) and maximum growth rate (Vmax).
Demonstrated how parameters influence fibril kinetics.
Established a predictive model for initial seed concentration.

Conclusions:

The model provides insights into amyloid propagation mechanisms.
Simulations can guide experiments for early disease detection.
Understanding filament kinetics is crucial for diagnosing amyloid diseases.