AVS 45th International Symposium
    Biomaterial Interfaces Group Tuesday Sessions
       Session BI+AS+MM+NS+SS-TuA

Invited Paper BI+AS+MM+NS+SS-TuA1
Self-Assembly of a Multidomain Protein: Fibronectin at Lipid Model Interfaces

Tuesday, November 3, 1998, 2:00 pm, Room 326

Session: Nanoscale to Mesocale Biomaterial Structures
Presenter: V. Vogel, University of Washington
Authors: V. Vogel, University of Washington
G. Baneyx, University of Washington
Correspondent: Click to Email
Fibronectin, an adhesion protein with multiple recognition sites, mediates cell attachment to synthetic and biological surfaces. In solution, fibronectin exists in a globular state where most of its recognition sites are buried in the protein core. Surface adsorption induces conformational changes in the protein that expose many of these sites. Furthermore, it is known that on the surface of cells fibronectin assembles into detergent insoluble fibers, which are considered to be the main functional form of the protein. Fibronectin is hence a prime example of a protein with multiple recognition sites that can be regulated through environmental control. Unfortunately, the molecular pathways of activation and self-assembly are still poorly understood. We have recently found that fibronectin can self-assemble into fibrillar networks at receptor-free phospholipid monolayer interfaces under physiological conditions. This is a crucial observation since the paradigm in biology is that fibril assembly of fibronectin is mediated by membrane-bound receptor molecules. Availability of a simplified model system allows investigation of the molecular pathways by which appropriate surfaces can activate fibronectin and facilitate self-assembly.