Understanding the nanoparticle-biological interface is important for both biomedical applications and environmental implications of these materials. Molecular-level understanding of this interface requires molecular-level techniques. We present the use of nuclear magnetic resonance spectroscopy to examine the interaction of 15N-labeled a-synuclein, a protein whose secondary structure is correlated with neurodegenerative disease, with a standard set of gold nanoparticles. a-synuclein is known to exist as a random coil in solution, adopt alpha helical conformations upon binding to phospholipid vesicles, but form beta sheet structures when aggregating to form cytotoxic fibrils. Understanding how a-synuclein interacts with gold nanoparticles might lead to control of its shape and aggregation, and further enhance knowledge of neurodegenerative disease pathways.

Understanding protein-nanoparticle interactions at a molecular level

247th National Meeting (2014)

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