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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: Aug 23, 2025

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.

Amberley D Stephens¹, Johanna Kölbel¹, Rani Moons²

¹Department of Chemical Engineering and Biotechnology, University of Cambridge, UK.

Angewandte Chemie (International Ed. in English)

|October 31, 2022

Summary

Solvation shell water mobility impacts amyloid protein aggregation. Reduced water mobility accelerates alpha-synuclein aggregation, a key factor in Parkinson's disease.

Keywords:

Amyloid Hydration Shell Hydrogen Bond Solvation Shell Solvent

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Area of Science:

Biochemistry
Physical Chemistry
Neuroscience

Background:

The solvation shell is critical for protein folding and function.
Its role in protein misfolding and aggregation, particularly in diseases like Parkinson's, remains unclear.

Purpose of the Study:

To investigate the influence of solvation shell water mobility on the aggregation rate of alpha-synuclein (αSyn).
To elucidate the mechanisms by which solvent properties affect αSyn aggregation.

Main Methods:

Studied the aggregation rates of αSyn under varying solvent conditions.
Utilized NaCl and CsI to modulate solvation shell water mobility.
Employed D2O as a solvent to assess solvent-driven effects.

Main Results:

Reduced solvation shell water mobility, induced by NaCl, increased αSyn aggregation rates.
Increased water mobility, induced by CsI, decreased αSyn aggregation rates.
Switching to D2O also increased aggregation rates, confirming a solvent effect.
Increased aggregation correlated with reduced mobility of both water and αSyn, not conformational changes.

Conclusions:

Solvation shell water mobility is a key determinant of αSyn aggregation rates.
Reduced mobility of both water and αSyn promotes aggregation by facilitating intermolecular interactions.
This finding offers new insights into the pathogenesis of Parkinson's disease.