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Protein aggregation is associated with many neurodegenerative diseases. We applied mid-infrared photothermal (MIP) to dissect the secondary structure of protein aggregates in living yeast cells modeling Huntington’s disease. We validated that MIP spectroscopy could reveal β-sheet enrichment by significant spectral changes and confirmed the β-sheet enrichment of aggregates in high throughput by wide-field fluorescence-detected MIP. By label-free identification of protein aggregates, we observed a further red shift in spectra for aggregates without GFP tag. Finally, by performing MIP spectroscopy with fine spatial steps, we discovered a partition of secondary structures between β-rich core and ɑ-rich shell of the aggregates.
Zhongyue Guo,Giulio Chiesa,Jiaze Yin,Adam Sanford,Stefan Meier,Ahmad S. Khalil, andJi-Xin Cheng
"Nanoscale structural mapping of protein aggregates in live cells modeling Huntington's disease by mid-infrared photothermal microscopy", Proc. SPIE PC12855, Advanced Chemical Microscopy for Life Science and Translational Medicine 2024, PC128550Z (13 March 2024); https://doi.org/10.1117/12.3000552
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Zhongyue Guo, Giulio Chiesa, Jiaze Yin, Adam Sanford, Stefan Meier, Ahmad S. Khalil, Ji-Xin Cheng, "Nanoscale structural mapping of protein aggregates in live cells modeling Huntington's disease by mid-infrared photothermal microscopy," Proc. SPIE PC12855, Advanced Chemical Microscopy for Life Science and Translational Medicine 2024, PC128550Z (13 March 2024); https://doi.org/10.1117/12.3000552