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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,...

Amyloid Fibrils

Amyloid Fibrils

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Updated: Mar 9, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Two-Step Amyloid Aggregation: Sequential Lag Phase Intermediates.

Fabio Castello¹, Jose M Paredes¹, Maria J Ruedas-Rama^1,2

¹Dept. of Physical Chemistry, Faculty of Pharmacy, University of Granada, Cartuja Campus, 18071, Granada Spain.

Scientific Reports

|January 10, 2017

Summary

This summary is machine-generated.

Nonspecific protein aggregates initiate amyloid fibril formation through a two-step mechanism. This study identifies key oligomeric intermediates and a critical conformational conversion step, revealing potential targets for preventing neurodegenerative diseases.

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Last Updated: Mar 9, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Area of Science:

Biochemistry
Neuroscience
Structural Biology

Background:

Amyloid fibril formation is central to neurodegenerative diseases like Alzheimer's and Parkinson's.
Oligomeric intermediates are implicated as toxic species in early aggregation phases.
Nonspecific interactions are hypothesized to initiate oligomerization, especially at low protein concentrations.

Purpose of the Study:

To investigate the role of nonspecific interactions in the early stages of amyloid aggregation.
To elucidate the molecular mechanism and identify key intermediates in amyloid formation.
To pinpoint cytotoxic species for therapeutic targeting.

Main Methods:

Advanced single-molecule fluorescence spectroscopy and imaging.
Mechanistic study of a model SH3 domain protein.
Characterization of oligomeric species based on size and compactness.

Main Results:

Direct evidence for nonspecific aggregates in a two-step nucleation mechanism of amyloid aggregation.
Identification of three distinct oligomeric types.
Discovery of a mandatory, rate-limiting conformational conversion step.

Conclusions:

Nonspecific aggregates are essential for initiating amyloid aggregation via a two-step process.
A conformational conversion step is critical for amyloid formation.
Identification of the most cytotoxic species offers potential therapeutic targets for neurodegenerative diseases.