UV light and other factors damage crystallin proteins in the eye lens, resulting in cataracts which scatter light and affect vision. Little information exists about protein structures within these disease-causing aggregates. We imaged postmortem lens tissue from individuals with and without cataracts using two-dimensional infrared (2DIR) spectroscopy. We distinguished diseased and healthy lens tissue by several 2DIR spectral signatures: diagonal intensity, anharmonicity, and cross peak frequency. Amyloid β-sheet secondary structure was detected in cataract lenses along with denatured structures. No amyloid structures were found in juvenile lenses, which have a high native β-sheet structure content. UV irradiation induces amyloid β-sheet structures in healthy lens tissue, which can be monitored using 2DIR. In addition, preliminary results will be shown testing the stabilities of crystallin amyloid fibrils formed under different aggregation conditions. We use a combination of 2DIR spectroscopic information and denaturation curves to correlate these observations.

Imaging amyloid structure in lens tissue using two-dimensional infrared spectroscopy

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.