AVS 50th International Symposium
    Biomaterial Interfaces Tuesday Sessions
       Session BI-TuP

Paper BI-TuP3
Non-Fouling Surfaces for Biosensors and Biomaterials

Tuesday, November 4, 2003, 5:30 pm, Room Hall A-C

Session: Poster Session
Presenter: L. Li, University of Washington
Authors: L. Li, University of Washington
S. Chen, University of Washington
J. Zheng, University of Washington
S. Jiang, University of Washington
Correspondent: Click to Email
Non-fouling surfaces are critical to the performance of biosensors and biomaterials. Despite of their importance and enormous effort, non-fouling mechanism is still not quite clear at present. It was shown in our previous work that the behavior of protein adsorption depended on nano-scale structures of a surface with which proteins interact. Therefore, molecular details of a surface are of great importance to protein adsorption. However, there is still a considerable lack of the fundamental understanding of how nano-scale structures affect protein adsorption at the molecular level. The objective of this work is to demonstrate that nano-scale structures of a surface are responsible for protein resistance. Polyethylene glycol (PEG) self-assembled monolayers (SAMs) are used as model systems and the nano-scale structures of the surfaces are altered by adjusting factors such as the assembly substrates, the assembly conditions, and the composition of mixed SAMs. These SAMs are characterized by atomic force microscopy (AFM)/scanning tunneling microscopy (STM) and X-ray photoelectron spectroscopy (XPS). Protein adsorption on these surfaces was investigated by surface plasmon resonance (SPR) biosensors and tapping-mode AFM. Furthermore, experimental results are directly compared with those from molecular simulations, which can also provide additional information not easily accessible to current laboratory experiments, such as adsorbed water structures at protein/SAM interfaces. Results from combined experimental and simulation studies provide insight on how nano-scale structures affect protein adsorption and shed light on non-fouling mechanisms.