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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...

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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

Discrimination between Alpha-Synuclein Protein Variants with a Single Nanometer-Scale Pore.

Mazdak Afshar Bakshloo¹, Safia Yahiaoui¹, Matthieu Bourderioux²

¹CY Cergy Paris Université, CNRS, LAMBE, Cergy 95000, France.

ACS Chemical Neuroscience

|June 29, 2023

Summary

This study shows a novel nanopore method can distinguish wild-type alpha-synuclein from its disease-associated E46K mutation and post-translational modifications, aiding neurodegenerative disease research.

Keywords:

Parkinson’s disease alpha-synuclein nanopores post-translational modifications protein identification

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

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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:

Neuroscience
Biochemistry
Nanotechnology

Background:

Alpha-synuclein aggregation is implicated in neurodegenerative diseases like Parkinson's.
Mutations and post-translational modifications alter alpha-synuclein structure and function.
Nanopore technology offers potential for protein discrimination.

Purpose of the Study:

To investigate if nanopore sensing can differentiate wild-type alpha-synuclein from specific variants.
To assess the method's capability in identifying alpha-synuclein mutations and post-translational modifications.

Main Methods:

Utilized a single nanometer-scale pore for protein analysis.
Applied the nanopore method to discriminate between wild-type alpha-synuclein, the E46K mutant, and modified forms (nitration, phosphorylation).

Main Results:

Successfully discriminated between wild-type alpha-synuclein and the E46K point mutation.
Demonstrated the ability to differentiate post-translationally modified alpha-synuclein (Y39 nitration, S129 phosphorylation).
Validated nanopore sensing as a tool for analyzing alpha-synuclein variants.

Conclusions:

Nanopore technology provides a sensitive method for characterizing alpha-synuclein.
This approach can identify disease-relevant alpha-synuclein alterations.
Potential applications in diagnosing and understanding neurodegenerative diseases.