title: Single-molecule dynamic force spectroscopy of the fibronectin-heparin interaction.
abstract: The integrity of cohesive tissues strongly depends on the presence of the extracellular matrix, which provides support and anchorage for cells. The fibronectin protein and the heparin-like glycosaminoglycans are key components of this dynamic structural network. In this report, atomic force spectroscopy was used to gain insight into the compliance and the resistance of the fibronectin-heparin interaction. We found that this interaction can be described by an energetic barrier width of 3.1+/-0.2A and an off-rate of 0.2+/-0.1s(-1). These dissociation parameters are similar to those of other carbohydrate-protein interactions and to off-rate values reported for more complex interactions between cells and extracellular matrix components. Our results indicate that the function of the fibronectin-heparin interaction is supported by its capacity to sustain significant deformations and considerable external mechanical forces.
authors.affiliation: Centre d'Etude et de Valorisation de la Diversité Microbienne (CEVDM), Département de biologie, Faculté des sciences, Université de Sherbrooke, Sherbrooke, Que., Canada J1K 2R1.
authors.forename: Gabriel
authors.initials: G
authors.lastname: Mitchell
authors.forename: Charles-Antoine
authors.initials: CA
authors.lastname: Lamontagne
authors.forename: Réjean
authors.initials: R
authors.lastname: Lebel
authors.forename: Michel
authors.initials: M
authors.lastname: Grandbois
authors.forename: François
authors.initials: F
authors.lastname: Malouin
mesh_terms: D001665:Binding Sites; D003198:Computer Simulation; D005353:Fibronectins / Q000737:chemistry* / Q000648:ultrastructure*; D006493:Heparin / Q000737:chemistry* / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D011485:Protein Binding; D013314:Stress, Mechanical
chemical_list: D005353:Fibronectins; D006493:Heparin