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Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Published on: October 24, 2017

X-ray diffraction from intact tau aggregates in human brain tissue.

Eric C Landahl¹, Olga Antipova, Angela Bongaarts

¹DePaul University, Department of Physics, 2219 N. Kenmore Ave., Chicago, IL 60614.

Nuclear Instruments & Methods in Physics Research. Section A, Accelerators, Spectrometers, Detectors and Associated Equipment

|August 31, 2011

Summary

This study introduces a new instrument combining fluorescence microscopy and X-ray diffraction to analyze brain tissue. It detects tau protein pathology in Pick's disease, revealing unique structural patterns in diseased areas.

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Area of Science:

Neuroscience
Biophysics
Pathology

Background:

Pick's disease is characterized by tau protein pathology.
Detecting tau protein in brain tissue is crucial for diagnosis.
Existing methods for tau protein analysis have limitations.

Purpose of the Study:

To develop and demonstrate an instrument for in-situ X-ray diffraction analysis of human brain tissue.
To specifically label and detect tau protein pathology using thiazine red fluorescence.
To investigate the structural properties of tau protein aggregates in diseased brain regions.

Main Methods:

Combined in-line visible light fluorescence microscopy with an X-ray diffraction microprobe.
Utilized thiazine red fluorescence to label filamentous tau protein.
Recorded X-ray diffraction patterns from selected regions of human brain tissue.

Main Results:

Thiazine red-labeled regions in diseased brain tissue exhibited distinct X-ray diffraction patterns.
Healthy brain tissue did not show these observed periodic structures.
A periodicity of 4.2 Å was identified, indicative of cross-beta sheet structure.

Conclusions:

The developed instrument can differentiate diseased from healthy brain tissue based on structural patterns.
The findings support the presence of cross-beta sheet structure in tau protein aggregates in Pick's disease.
This technique offers a novel approach for studying protein misfolding diseases.