The Detection of Amyloid-Beta Neuroplaques Using Thioflavin T and Secondary Ion Mass Spectrometry

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Abstract

Secondary ion mass spectrometry excels at determining the spatialdistribution of lipids in tissue, and thus has been used as a tool to elucidate thepathophysiologic mechanisms/etiology of Alzheimer’s disease. However, secondaryion mass spectrometry struggles to detect larger macromolecules such as thecharacteristic protein plaques associated with Alzheimer’s disease. This project wasundertaken to determine a protocol that would identify Alzheimer’s amyloid plaquesusing secondary ion mass spectrometry and then compare the plaque location to thelipid distribution within the diseased brain tissue. To accomplish this, samples werestained using Thioflavin T, a fluorescent molecule whose size is within theinstrument's range of detection and that specifically binds to amyloid plaques. Thesamples were then analysed with secondary ion mass spectrometry to detect thecharacteristic fragment of Thioflavin T. This method proved successful and allowedfor the comparison of amyloid plaque locations with the spatial distribution ofvarious lipid species.

Layman's Abstract

Using secondary ion mass spectroscopy provides unique spatial determination of lipids and molecules in tissue samples, yet this technique is unable to identify larger proteins. Thus, in order to identify the very large, hallmark plaques of Alzheimer's disease, a novel approach had to be developed. By using a small-molecular-weight molecule that binds to these hallmark plaques, we were able to identify where in the tissue these plaques were located using Secondary Ion Mass Spectroscopy.

Keyword(s)

Secondary Ion Mass Spectroscopy

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