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

DePaul University, Department of Physics, 2219 N. Kenmore Ave., Chicago, IL 60614.
Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment (Impact Factor: 1.32). 09/2011; 649(1):184-187. DOI: 10.1016/j.nima.2011.01.059
Source: PubMed

ABSTRACT We describe an instrument to record x-ray diffraction patterns from diseased regions of human brain tissue by combining an in-line visible light fluorescence microscope with an x-ray diffraction microprobe. We use thiazine red fluorescence to specifically label and detect the filamentous tau protein pathology associated with Pick's disease, as several labs have done previously. We demonstrate that thiazine red-enhanced regions within the tissue show periodic structure in x-ray diffraction that is not observed in healthy tissue. One observed periodicity (4.2 Å) is characteristic of cross-beta sheet structure, consistent with previous results from powder diffraction studies performed on purified, dried tau protein.

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Available from: Thomas C Irving, Jun 27, 2015
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