Single-molecule dynamic force spectroscopy of the fibronectin-heparin interaction
- Centre d'Etude et de Valorisation de la Diversite Microbienne (CEVDM), Departement de biologie, Faculte des sciences, Universite de Sherbrooke, Sherbrooke, Que., J1K 2R1 (Canada)
- Departement de pharmacologie, Faculte de medecine et des sciences de la sante, 3001, 12 avenue nord, Universite de Sherbrooke, Sherbrooke, Que., J1H 5N4 (Canada)
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 {+-} 0.2 A and an off-rate of 0.2 {+-} 0.1 s{sup -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.
- OSTI ID:
- 21033020
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 364, Issue 3; Other Information: DOI: 10.1016/j.bbrc.2007.10.034; PII: S0006-291X(07)02205-X; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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