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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...

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: Jun 24, 2026

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis.

Allen W Bryan¹, Matthew Menke, Lenore J Cowen

¹Harvard/MIT Division of Health Science and Technology, Bioinformatics and Integrative Genomics, Cambridge, Massachusetts, USA.

Plos Computational Biology

|March 28, 2009

Summary

This summary is machine-generated.

BETASCAN predicts beta-structures in amyloids and prion proteins by analyzing beta-strands and strand-pairs. This computational tool accurately identifies protein structures and heterogeneity, aiding in understanding diseases like amyloidosis.

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Last Updated: Jun 24, 2026

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Published on: March 7, 2019

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Area of Science:

Structural biology
Computational biology
Biophysics

Background:

Amyloids and prion proteins are critical beta-structures with complex supersecondary structures challenging to determine experimentally or computationally.
Significant conformational heterogeneity is often observed in amyloid fibrils, complicating structural analysis.

Purpose of the Study:

To develop a novel computational strategy for predicting beta-structure, focusing on beta-strands and strand-pairs as fundamental units.
To introduce BETASCAN, a program designed to predict beta-structure and amyloid propensity with improved accuracy and sensitivity.

Main Methods:

Developed a new beta-structure prediction strategy using pairwise probabilistic statistics.
Implemented BETASCAN, a program that calculates likelihood scores for potential beta-strands and strand-pairs based on parallel beta-sheet correlations.
BETASCAN suggests multiple alternate folding patterns and assigns relative probabilities based on amino acid sequence and pre-chosen parameters.

Main Results:

BETASCAN demonstrates favorable comparison with existing algorithms in beta-structure and amyloid propensity prediction.
Accurate predictions were achieved for experimentally determined amyloid beta-structures, known beta-aggregates, and parallel beta-strands in beta-helices.
The program successfully detected competing structures for proteins with contradictory experimental data, such as Abeta and Het-s.

Conclusions:

BETASCAN offers a sensitive and accurate method for predicting beta-strands and their edges, even in complex sequences.
The ability to identify multiple potential beta-structures computationally facilitates the investigation of prion strains and amyloid structural heterogeneity.
BETASCAN is publicly available online, providing a valuable tool for researchers in structural biology and disease mechanism studies.