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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,...

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Related Experiment Video

Updated: Mar 17, 2026

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods.

Damien Hall¹, Ran Zhao², Masatomo So³

¹Research School of Chemistry, Australian National University, Acton ACT 2601, Australia; Institute for Protein Research, Osaka University, 3-1- Yamada-oka, Suita, Osaka 565-0871 Japan.

Analytical Biochemistry

|July 20, 2016

Summary

This summary is machine-generated.

This study introduces methods to simulate and analyze variable amyloid formation kinetics. Understanding this variability is crucial for developing effective anti-amyloid therapies in drug trials.

Keywords:

Aggregation assay Amyloid Anti-amyloid drug screening Statistical significance

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Last Updated: Mar 17, 2026

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Area of Science:

Biochemistry and Biophysics
Pharmacology and Drug Discovery

Background:

Amyloid formation is a complex process with inherent kinetic variability.
This variability poses challenges in accurately assessing drug efficacy.

Purpose of the Study:

To develop and validate methods for simulating, identifying, and analyzing kinetic variability in amyloid formation.
To enhance the interpretation of kinetic data for drug discovery and development.

Main Methods:

Simulated amyloid formation kinetics using an irreversible nucleation-growth model with randomly sampled rate constants.
Reduced complex kinetic traces to three characteristic parameters.
Applied bootstrap procedures and statistical tests to assess parameter distribution convergence and significance of shifts.

Main Results:

Demonstrated methods for simulating and analyzing intrinsic variability in amyloid formation kinetics.
Validated statistical approaches for assessing parameter distribution convergence under varying levels of intrinsic variation.
Showcased the utility of robust analysis methods for interpreting kinetic data with significant variance.

Conclusions:

Robust methods for analyzing variable amyloid formation kinetics are essential for accurate drug screening.
Improved understanding of kinetic variability will facilitate more rigorous evaluation of anti-amyloid compounds in clinical trials.