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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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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

Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces.

Steven J Roeters^1,2, Kris Strunge³, Kasper B Pedersen³

¹Department of Chemistry, Aarhus University, Langelandsgade 140, 8000, Aarhus C, Denmark. s.j.roeters@amsterdamumc.nl.

Nature Communications

|September 18, 2023

Summary

Lipid membranes influence Parkinson's disease-related alpha-synuclein (αS) aggregation. Elevated concentrations cause αS to adopt an upright conformation, promoting interactions and amyloid formation.

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Area of Science:

Biophysics
Neuroscience
Structural Biology

Background:

Amyloid aggregation of alpha-synuclein (αS) is linked to Parkinson's disease.
Lipid membranes can catalyze αS aggregation, but the detailed structure of membrane-bound αS is unknown.

Purpose of the Study:

To investigate the structure and orientation of monomeric αS bound to anionic lipid interfaces.
To understand how αS-lipid ratios affect binding and conformation.

Main Methods:

Interface-specific vibrational sum-frequency generation (VSFG) experiments.
Out-of-equilibrium molecular dynamics simulations with a novel frame-selection method ('ViscaSelect').
Excitonic spectral calculations to compare simulations with experimental data.

Main Results:

At low and physiological αS concentrations, αS adopts a flat-lying helical structure.
At elevated, potentially disease-related concentrations, αS transitions to an upright, interface-protruding conformation.
This upright conformation promotes lateral αS monomer interactions.

Conclusions:

The study reveals concentration-dependent structural transitions of αS at lipid interfaces.
Upright αS conformations at elevated concentrations may explain lipid-mediated amyloid catalysis in Parkinson's disease.
Findings provide structural insights into αS aggregation mechanisms at membrane surfaces.