IUVSTA 15th International Vacuum Congress (IVC-15), AVS 48th International Symposium (AVS-48), 11th International Conference on Solid Surfaces (ICSS-11)
    Biomaterials Thursday Sessions
       Session BI-ThP

Paper BI-ThP2
Protein Adsorption on Mixed Self-assembled Monolayers

Thursday, November 1, 2001, 5:30 pm, Room 134/135

Session: Biomolecule and Cell Poster Session
Presenter: L. Li, University of Washington
Authors: L. Li, University of Washington
S. Chen, University of Washington
C. Boozer, University of Washington
S. Jiang, University of Washington
Correspondent: Click to Email
Mixed self-assembled monolayers (SAMs) of alkanethiols on Au(111) can be used to precisely control molecular-scale chemical, structural, and biological surface properties via controlling the abundance, the type, and the spatial (both normal and lateral) distribution of tail group sites. By controlling surface microenvironment, different structures and activities of immobilized proteins are expected. Here, we first report our recent studies on phase behavior of mixed alkanethiols with two compounds having different chain lengths (C8-C18) and terminal groups (-COOH, -OH, -CH@sub 3@, and -NH@sub 2@) on Au(111). These mixed SAMs are characterized by scanning tunneling microscopy (STM) and atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS), contact angle measurements, and ellipsometry. Results show that closely packed and homogeneously mixed SAMs can be achieved at the molecular level. These controlled surfaces will then be used for the adsorption of various proteins such as albumin, lysozyme, etc. Adsorption behavior is characterized by tapping-mode AFM and surface plasmon resonance (SPR) sensors. Results show that molecular-scale mixed SAMs generally promote protein adsorption. The effect of the abundance, type, and spatial distribution of terminal groups on protein adsorption is explored systematically in this work. Keywords: Mixed SAMs, protein adsorption, AFM, SPR, and XPS.