Gold nanoparticles (AuNPs) have been of interest due to their biocompatibility and surface plasmon resonance. Biomolecules can spontaneously adsorb to their surface, a trait that could be exploited for drug targeting. It is unclear, however, whether protein-AuNP interactions at the nanoparticle surface are dependent on nanoparticle size. In this project, we investigate whether surface curvature can induce protein unfolding and multilayer binding in citrate-coated AuNPs of various sizes. An NMR-based approach was utilized to determine the adsorption capacity, and protein NMR spectra were compared to determine whether nanoparticle size influences protein interactions. Transmission electron microscopy (TEM) was used to support the results. Over a range of AuNP sizes (15-100 nm) proteins appear globular on the nanoparticle surface. Additionally, a single layer of proteins is adsorbed regardless of AuNP size. Our results are consistent for two differently sized proteins, GB3 (6 kDa) and bovine carbonic anhydrase (BCA, 29 kDa).
| Identifer | oai:union.ndltd.org:MSSTATE/oai:scholarsjunction.msstate.edu:td-3875 |
| Date | 14 August 2015 |
| Creators | Woods, Karen Elizabeth |
| Publisher | Scholars Junction |
| Source Sets | Mississippi State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
Page generated in 0.002 seconds