| AVS 55th International Symposium & Exhibition | |
| Biomaterial Interfaces | Tuesday Sessions |
| Session BI+NC-TuA |
| Session: | Protein and Cells Interactions on Micro- and Nanofabricated Substrates |
| Presenter: | S.P. Sullivan, University of Delaware |
| Authors: | S.P. Sullivan, University of Delaware X. Zhang, University of Delaware M.E. Boggs, University of Delaware H.P. Bui, University of Delaware A.V. Teplyakov, University of Delaware T.P. Beebe, Jr., University of Delaware |
| Correspondent: | Click to Email |
Biological and chemical surface modifications at the nanoscale have become a large area of research in response to the need for new and improved applications such as biochemical sensors and medical implants. The work describe here investigates the important extracellular matrix protein, Laminin onto Si(111) and templated silicon nanostructures. These substrates are being evaluated as biomaterial bridges for neuron outgrowth. The nanostructures are templated onto the surface of highly oriented pyrolytic graphite using “molecule corrals,” which are nanometer-sized (1 – 100 nm diameter) structures etched into the basal plane of graphite. The intial defects from which molecule corrals originate are routinely produced using a low-energy cesium ion beam, followed by thermal oxidation at 650 ˚C. Using a physical vapor deposition method, silicon is then deposited onto the HOPG, leading to the formation of billions of silicon nanostructures. Previous results suggest that these structures will react similar to that of hydrogen-terminated silicon single crystal wafers. A comparison with a new protein attachment scheme, beginning with a self-assembled monolayer of 11-amino-1-undecene, was completed. XPS, TOF-SIMS, and AFM were used to characterize the substrates following each step of the reaction. To avoid deposition of physically adsorbed protein, careful rinsing and sonication procedures were optimized and used. From these results it was determined that the nanostructures react similarly to the hydrogen-terminated Si(111) surface for this covalent attachment scheme, and that protein attachment was successful on the nanostructures. To evaluate the reaction efficiency, an additional study comparing two covalent protein attachment schemes on silicon nanostructures is underway.