AVS 46th International Symposium
    Biomaterial Interfaces Group Tuesday Sessions
       Session BI-TuM

Paper BI-TuM2
Hierarchical Ordering of Proteins at Interfaces with a Nanoscale Surface Topography

Tuesday, October 26, 1999, 8:40 am, Room 613/614

Session: Protein Solid-Surface Interactions II
Presenter: V. Vogel, University of Washington
Authors: V. Vogel, University of Washington
L. Smith, University of Washington
T. Nguyen, University of Washington
J.R. Dennis, University of Washington
Correspondent: Click to Email
Elucidating mechanisms by which to control the ordering of proteins at interfaces is of fundamental importance in bioengineering and biotechnology. Whereas major progress has been made recently in stabilizing proteins at interfaces in their native states, and in controlling their orientation, much less is known how to promote their spontaneous self-assembly into a structurally well controlled supramolecular architecture. Here we discuss that nanoscale topographic surface features with ridges the size of natural ECM fibrils have a pronounced impact on protein adsorption, and on the spatial alignment of human dermal fibroblasts and cell-deposited collagen fibrils. Furthermore, by elevating cells above the surface such that they deposit collagen through a porous membrane onto the nanoscale ridges without being in physical contact with the surface, the role of the cells has been separated from the role of topography in collagen type VI deposition and fibrillogenesis. Insight into the mechanisms by which synthetic surfaces manipulate the hierarchical organization of ECM fibrils will be crucial in the rational design of the surface topography of biomaterials and of scaffolds for tissue engineering.