Nanoscale investigation of protein-surface interactions using scanning probe microscopy

COLL 539

Cindy L. Berrie, Katherine L. Marchin, and Jill E. Headrick. Department of Chemistry, University of Kansas, 1251 Wescoe Hall Drive Rm 1027, Department of Chemistry, Malott Hall, Lawrence, KS 66045
The interactions of fibrinogen with surfaces have been studied using atomic force microscopy (AFM). Well-characterized model substrates have been used to investigate the effect of surface chemistry and structure on the adsorption of fibrinogen. In one example, 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. These 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 more information than simply topography.