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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...

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...

Alzheimer Disease ll: Pathophysiology

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...

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Related Experiment Video

Updated: May 27, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

Segmental polymorphism in a functional amyloid.

Kan-Nian Hu¹, Ryan P McGlinchey, Reed B Wickner

¹Laboratory of Chemical Physics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.

Biophysical Journal

|November 10, 2011

Summary

This summary is machine-generated.

Amyloid fibrils, like those from Pmel17, can have biological roles and exhibit diverse molecular structures. Even functional amyloid fibrils show segmental polymorphism, where different protein segments form the fibril core.

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

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Last Updated: May 27, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Published on: October 17, 2015

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:

Biophysics
Structural Biology
Biochemistry

Background:

Amyloid fibrils are implicated in diseases but can also perform biological functions.
Pmel17 fibrils in melanosomes serve as a template for melanin deposition, highlighting functional amyloid roles.

Purpose of the Study:

To investigate the structural polymorphism of Pmel17:RPT fibrils.
To determine if biological function correlates with a unique fibril structure.

Main Methods:

Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
Analysis of three Pmel17:RPT polymorphs.
Monte Carlo assignment algorithm for protein segment identification.

Main Results:

Pmel17:RPT fibrils exhibit structural polymorphism across biologically relevant pH ranges.
A subset (~30%) of the amino acid sequence forms the fibril core, varying between polymorphs.
Segmental polymorphism, where core-forming segments differ among polymorphs, was observed.

Conclusions:

Functional amyloid fibrils do not require a single, unique molecular structure.
Segmental polymorphism is a characteristic of Pmel17:RPT fibrils, influencing their structure and potentially function.