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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: Jul 20, 2025

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

Lipid-induced polymorphic amyloid fibril formation by α-synuclein.

Bhanu P Singh^1,2, Ryan J Morris¹, Tilo Kunath³

¹School of Physics and Astronomy, The University of Edinburgh, Edinburgh, UK.

Protein Science : a Publication of the Protein Society

|July 29, 2023

Summary

Lipid membranes accelerate alpha-synuclein aggregation and promote diverse amyloid fibril structures. This study reveals how membrane interfaces influence fibril formation and morphology, impacting disease pathways.

Keywords:

amyloid polymorphism lipid-protein interaction polypeptide self-assembly protein aggregation α-synuclein

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Last Updated: Jul 20, 2025

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

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Published on: August 16, 2020

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Area of Science:

Biochemistry
Neuroscience
Materials Science

Background:

Proteins self-assemble into amyloid fibers, which can exist in diverse polymorphic forms.
Amyloid polymorphs exhibit varying toxicity and are linked to different disease conditions.
Factors driving amyloid fibril polymorphism remain largely unknown.

Purpose of the Study:

To investigate the role of lipid membranes in alpha-synuclein amyloid aggregation.
To determine if lipid interfaces influence the diversity of amyloid fibril morphologies.
To explore the incorporation of lipids into alpha-synuclein fibrils.

Main Methods:

Utilized 1,2-dimyristoyl-sn-glycero-3-phospho-L-serine (a neuronal plasma membrane lipid) in alpha-synuclein aggregation experiments.
Analyzed the morphological diversity of resulting amyloid fibrils using high-resolution imaging techniques.
Confirmed lipid incorporation into the formed amyloid structures.

Main Results:

The presence of the lipid markedly accelerated alpha-synuclein aggregation.
A wide range of polymorphic forms, including fibrils, ribbons, nanotubes, and sheets, were generated under identical conditions.
Amyloid fibrils were found to incorporate lipid molecules into their structures.
Lipid interfaces were shown to modulate aggregation kinetics and induce morphological variations.

Conclusions:

Lipid membranes can significantly accelerate alpha-synuclein amyloid aggregation.
Membrane interfaces play a crucial role in generating diverse amyloid fibril polymorphs.
Lipid incorporation into fibrils suggests a mechanism for altered fibril properties and potential disease relevance, as seen in Lewy bodies.