title: Atomic force microscope studies of fibrinogen adsorption.
abstract: Since its invention in 1986 by Binnig, Quate, and Gerber, the atomic force microscope (AFM) has proven to be an extremely useful tool for examining the interactions of proteins with surfaces. Fibrinogen in particular has been used as a model protein to demonstrate new methodologies for studying protein behavior with AFM due to its unique size, shape, and function. Indeed, fibrinogen's central role in both blood coagulation and blood-based infections has made it the primary protein used to interrogate the biocompatibility of surfaces. The goal of this review is to provide an analytical perspective on the utility of AFM for investigating the interaction of fibrinogen with surfaces.
authors.affiliation: Department of Physics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
authors.forename: Laurel E
authors.initials: LE
authors.lastname: Averett
authors.forename: Mark H
authors.initials: MH
authors.lastname: Schoenfisch
mesh_terms: D000327:Adsorption; D005340:Fibrinogen / Q000737:chemistry* / Q000648:ultrastructure; D018625:Microscopy, Atomic Force / Q000379:methods*; D013499:Surface Properties
chemical_list: D005340:Fibrinogen