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-ThM

Paper BI-ThM4
Deformation of Proteins Adsorbed on Glass Surfaces as Characterized by XAS

Thursday, November 1, 2001, 9:20 am, Room 102

Session: Protein Surface Interaction
Presenter: H.E. Canavan, George Washington University
Authors: H.E. Canavan, George Washington University
J.J. Hickman, Clemson University
W.E. O'Grady, U.S. Naval Research Laboratory
D.E. Ramaker, George Washington University
Correspondent: Click to Email
The interaction of proteins with artificial surfaces is of interest to many in the fields of medicine, biotechnology, and surface science. It is known that certain proteins experience considerable conformational deformation upon adsorption onto surfaces. In contrast, some proteins are described as colloidal or "hard," and experience little if any deformation upon adsorption. In the work presented here, the biomolecular interaction is characterized by X-Ray Absorption Spectroscopy (XAS). Sulfur K-edge XAS will be used to analyze the S-S, S-C and S-O bonds to monitor the extent to which the sulfur bond character is changed in both "hard" and "soft" proteins such as BSA, lysozyme, and cytochrome C upon their adsorption onto a glass surface. In addition, X-ray Photoelectron Spectroscopy (XPS) is used to characterize the glass surfaces both prior and subsequent to protein deposition.