While nanoparticles have generated significant interest for their potential use as drug delivery systems, the health risks associated with exposure to nanoparticles are not yet well understood. Proteins in solution can bind to the surface of nanoparticles, often altering their structure to facilitate binding, which can result in functional consequences. As such, it is critical to elucidate these structural changes in order to better utilize nanoparticles in medical treatments, as well as to assess any unintended consequences of nanoparticle exposure. We are currently developing a method to monitor protein secondary structure in nanoparticle-bound proteins using two-dimensional infrared (2DIR) spectroscopy in combination with isotope labeling. 2DIR is an ultrafast vibrational technique that is highly sensitive to secondary structure and atomic mass. By strategically incorporating isotope labels into the protein backbone, it is possible to spectrally differentiate these labeled residues, allowing for the structure of small regions to be determined independently from the rest of the protein. We are currently testing various isotope labeling schemes on a model alpha-helical peptide, and the labeling scheme determined to be most sensitive to changes in alpha-helical structure will later be incorporated into larger and more complex systems.

Tracking structural changes in nanoparticle-bound proteins using 2D infrared spectroscopy

2019 Spring National Meeting

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