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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...

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Related Experiment Video

Updated: Jun 13, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Amyloid - membrane interactions: experimental approaches and techniques.

Raz Jelinek¹, Tania Sheynis

¹Department of Chemistry, Ben Gurion University, Beer Sheva 84105, Israel. razj@bgu.ac.il

Current Protein & Peptide Science

|April 29, 2010

Summary

This summary is machine-generated.

Lipid and membrane interactions are crucial in amyloid disease progression and toxicity. This review covers biophysical and biological techniques used to study these membrane-peptide interactions and their role in amyloidogenesis.

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

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Last Updated: Jun 13, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Area of Science:

Biochemistry
Biophysics
Cell Biology

Background:

Amyloid diseases involve toxic pathways where lipids and membranes play a central role.
Evidence shows lipid binding and membrane association of amyloidogenic peptides are critical for disease onset and progression.

Purpose of the Study:

To review experimental approaches for investigating amyloid peptide-membrane interactions.
To summarize techniques probing membrane contributions to fibrillation and amyloidogenesis.

Main Methods:

Biophysical techniques to study membrane-peptide interactions.
Biological assays to assess membrane-peptide interactions.
Review of recent experimental approaches.

Main Results:

Lipid binding and membrane association are key to amyloid disease pathology.
Membranes reciprocally influence amyloid fibrillation and amyloidogenesis.

Conclusions:

Understanding membrane-peptide interactions is vital for amyloid disease research.
Various biophysical and biological techniques are essential for studying these mechanisms.