Single-molecule dynamic force spectroscopy of the fibronectin-heparin interaction.
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.
Mitchell
Gabriel
G
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.
Lamontagne
Charles-Antoine
CA
Lebel
Réjean
R
Grandbois
Michel
M
Malouin
François
F
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
D005353:Fibronectins; D006493:Heparin