Quantification of AuNP-protein interaction using NMR

Friday, November 15, 2019


Sarah Claxton

Department of Chemistry

College of Arts & Sciences

The application of gold nanoparticles (AuNP) is an increasingly prominent research field that covers a wide range of techniques, including biosensing, drug and gene therapy, and bioimaging. When exposed to biological fluids, AuNPs will interact with proteins in solution, and these proteins will compete to bind to the AuNP surface. NMR has been the primary means of studying this biological interaction; specifically, 2D 1H-15N HSQC methods were used to visualize the protein interaction kinetics with nanoparticles. A 1H-15N HSQC technique was used to quantify AuNP binding versus time for a mixture of GB3 and Ubiquitin, two small model proteins. GB3 and Ubiquitin signals were sampled at several differing concentrations and an external standard was used to quantify absolute binding to the AuNPs. Our results suggest a mechanism by which nanoparticle surface character may change over time, and this may be an important consideration in the design of nanoparticle-based therapeutics. Currently our research is moving towards investigating more biologically relevant proteins, R2ab and Amidase.


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