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Related Experiment Video

Updated: Jun 18, 2026

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

Orthogonal Ionic Liquid-Based Extraction Strategy Enables Amyloid-Specific Profiling of Aggregate Proteome.

Shiying Zheng^1,2, Ye Liu³, Bowen Zhong^1,4

¹State Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)

|April 20, 2026

Summary

A new method selectively isolates amyloid aggregates from biological samples. This technique aids in understanding neurodegenerative diseases like Alzheimer's by revealing protein links to amyloid pathology.

Keywords:

Ionic liquids amyloid deposits neurodegenerative diseases orthogonal extraction proteome

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Published on: March 27, 2017

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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

Area of Science:

Biochemistry
Neuroscience
Proteomics

Background:

Amyloid deposits are key in neurodegenerative diseases but hard to study due to insolubility.
Characterizing amyloid composition and formation is crucial for understanding disease mechanisms.

Purpose of the Study:

To develop a method for selective enrichment and molecular profiling of amyloid aggregates.
To investigate the molecular composition and associated pathways of amyloid deposits in Alzheimer's disease models.

Main Methods:

Developed an orthogonal ionic liquid-based extraction strategy (Orth-iEA) using specific ionic liquids.
Utilized tetramethylguanidine tetrafluoroborate (TMGBF4) to solubilize amyloid and 1-dodecyl-3-methylimidazolium chloride (C12ImCl) for non-amyloid proteins.
Applied Orth-iEA to Alzheimer's disease mouse models for proteomic analysis via LC-MS/MS.

Main Results:

Orth-iEA successfully and selectively enriched amyloid aggregates from complex biological samples.
Identified numerous amyloid-associated proteins, many linked to mitochondrial components.
Functional analysis revealed connections between amyloid pathology and pathways like protein transport, mitochondrial translation, and apoptosis.

Conclusions:

Orth-iEA is an effective chemical platform for isolating and analyzing amyloid aggregates.
The study uncovered novel molecular links between amyloid pathology and Alzheimer's disease.
This method advances the study of amyloid-related neurodegenerative diseases.