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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: Jun 29, 2025

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle

Céline Galvagnion¹, Abigail Barclay², Katarzyna Makasewicz³

¹Department of Drug Design and Pharmacology, University of Copenhagen, 2100 Copenhagen, Denmark. celine.galvagnion@sund.ku.dk.

Physical Chemistry Chemical Physics : PCCP

|March 25, 2024

Summary

Lipids accelerate amyloid fibril formation by interacting with proteins like alpha-synuclein. This study reveals lipids actively restructure, forming particles that later assemble into amyloid fibrils.

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Last Updated: Jun 29, 2025

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

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Published on: May 30, 2021

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

Area of Science:

Biochemistry
Neuroscience
Materials Science

Background:

Amyloid fibrils are key in neurodegenerative diseases.
Lipid interactions accelerate amyloid formation, particularly primary nucleation.
The precise mechanism of lipid-accelerated amyloidogenesis remains unclear.

Purpose of the Study:

To investigate the structural mechanisms of alpha-synuclein binding to model lipid membranes.
To elucidate the role of lipids in the co-assembly into amyloid fibrils.
To understand how lipids influence the early stages of amyloid formation.

Main Methods:

Dynamic Light Scattering (DLS)
Small-Angle X-ray Scattering (SAXS)
Small-Angle Neutron Scattering (SANS)

Main Results:

Lipid membranes undergo significant structural changes upon alpha-synuclein binding.
Alpha-synuclein induces membrane break-up into small, disc- or rod-like lipid-protein particles.
These particles mature into amyloid fibrils over time, incorporating lipids.

Conclusions:

Model membranes play an active role in alpha-synuclein amyloidogenesis.
Lipid-protein particle intermediates are crucial for fibril formation.
Understanding these interactions may offer therapeutic targets for neurodegenerative diseases.