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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...

The Proteasome

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Microtubule Associated Proteins (MAPs)

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
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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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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Related Experiment Video

Updated: May 12, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 6, 2013

Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.

Heidi Olzscha¹, Sonya M Schermann, Andreas C Woerner

¹Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.

|January 11, 2011

Summary

Artificial protein aggregates cause disease by disrupting essential cellular functions. This study reveals that toxic aggregates sequester large, unstructured proteins, leading to multifactorial cellular collapse and neurodegeneration.

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Last Updated: May 12, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

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Published on: December 6, 2013

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Area of Science:

Biochemistry
Cell Biology
Neuroscience

Background:

Protein aggregation, particularly amyloid-like fibril formation, is implicated in neurodegeneration and other diseases.
The precise mechanisms driving the toxicity of these aggregates remain poorly understood.

Purpose of the Study:

To investigate the gain-of-function toxicity of artificial β sheet proteins designed to form amyloid-like fibrils.
To identify the cellular targets and pathways affected by these toxic protein aggregates.

Main Methods:

Quantitative proteomics was employed to analyze protein interactions and cellular responses.
Artificial β sheet proteins were designed to form amyloid-like fibrils in human cells.

Main Results:

Aggregate toxicity correlated with the promotion of aberrant protein interactions and deregulation of the cytosolic stress response.
Endogenous proteins sequestered by aggregates were large, enriched in unstructured regions, and functionally multifunctional.
Interacting proteins included essential hubs involved in chromatin organization, transcription, translation, cell architecture, and protein quality control.

Conclusions:

Amyloidogenic aggregation targets a specific subproteome characterized by large size and unstructured regions.
This targeting leads to multifactorial toxicity by disrupting essential cellular networks.
The collapse of these critical cellular functions contributes to disease pathogenesis.