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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

Protein Organization

Protein Organization

Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

Updated: Dec 23, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Amyloid Evolution: Antiparallel Replaced by Parallel.

Ali Asghar Hakami Zanjani¹, Nicholas P Reynolds², Afang Zhang³

¹Department of Physics and Materials Science, University of Luxembourg, Luxembourg City, Luxembourg.

Biophysical Journal

|April 21, 2020

Summary

This summary is machine-generated.

Amyloid fibrils initially form antiparallel structures, contrary to common belief. This early antiparallel structure transitions to parallel forms in larger amyloid aggregates, impacting disease mechanisms and therapeutic design.

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Last Updated: Dec 23, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

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Published on: December 5, 2013

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Published on: September 17, 2017

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Published on: March 21, 2025

Area of Science:

Biophysics
Structural Biology
Neuroscience

Background:

Micrometer-scale amyloid fibrils often exhibit parallel β-sheet structures.
Nanometer-scale amyloid assemblies are implicated in cytotoxicity and disease contagion.
Understanding early aggregation structures is crucial for therapeutic development.

Purpose of the Study:

To investigate the initial structural organization of aggregating peptides.
To determine if antiparallel structures precede parallel structures in amyloid formation.
To inform the design of therapeutics targeting amyloid nucleation and spread.

Main Methods:

Solution X-ray scattering combined with molecular dynamics simulations.
Analysis of peptide aggregation at early and late stages.
Literature review of amyloid structures and formation pathways.

Main Results:

Antiparallel β-sheet structures dominate the initial stages of aggregation for specific peptides.
Parallel β-sheet structures become prevalent only in larger, micrometer-scale aggregates.
This structural divergence suggests a common initial antiparallel phase in amyloid formation.

Conclusions:

The initial structure of amyloid aggregates is predominantly antiparallel, not parallel.
This finding challenges existing models and highlights the importance of early aggregation states.
Targeting antiparallel structures could offer novel therapeutic strategies for amyloid diseases.