Tracking Aggregation and Fibrillation of Globular Proteins Using Terahertz and Far-Infrared Spectroscopies
作者： Gretel M. Png , Robert J. Falconer , Derek Abbott
DOI: 10.1109/TTHZ.2015.2505900
关键词:
摘要: Partially unfolded proteins can self-assemble to form insoluble protein fibrils with diameters in the nanometer scale. These are of particular interest healthcare because their presence diseases such as Alzheimer's disease and type-II diabetes. Tracking formation has far-reaching benefits for research into treatment these diseases. Current optical techniques that track fibrillation either limit samples aqueous or slow conduct. We present this work terahertz far-infrared (FIR) spectroscopic analyses made from three globular proteins. process over an extended period show mature have distinct absorbance properties not solely caused by scattering. Results also FIR spectroscopy provide information about fibril structures is otherwise missed techniques.
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