AVS 51st International Symposium
    Biomaterial Interfaces Monday Sessions
       Session BI-MoA

Paper BI-MoA9
The Effect of Surface Structure and Functionality on Conformation of Surface-Adsorbed Fibrinogen

Monday, November 15, 2004, 4:40 pm, Room 210D

Session: Protein-Surface Interactions
Presenter: C.L. Berrie, University of Kansas
Authors: C.L. Berrie, University of Kansas
J.E. Headrick, University of Kansas
K.L. Marchin, University of Kansas
S. Phung, University of Kansas
Correspondent: Click to Email
The interactions of the plasma protein fibrinogen with surfaces have been studied using atomic force microscopy (AFM). Specifically, well-characterized model substrates have been used to investigate the effect of surface chemistry and structure on the adsorption of fibrinogen. Dramatic differences in the average size and shape of fibrinogen molecules adsorbed to hydrophobic and hydrophilic substrates have been observed. These changes can be readily seen in AFM images of individual molecules with sub-molecular resolution. The differences have been quantified and correlated with the surface chemistry. In addition, new methods for patterning nanostructured substrates for use in these experiments have been investigated as well as methods for chemically functionalizing AFM probe tips in order to obtain information beyond topography. Adsorption of fibrinogen on nanostructured thin films and the effects of ionic strength and pH of the solution will also be discussed.