Kennelly, T.M., Li, Y., Cao, Y. et al. (2 more authors) (2019) Distinct binding interactions of α5β1-integrin and proteoglycans with fibronectin. Biophysical Journal, 117 (4). pp. 688-695. ISSN 0006-3495
Abstract
Dynamic single molecule force spectroscopy was performed to monitor the unbinding of fibronectin with the proteoglycans syndecan-4 and decorin, and to compare this with the unbinding characteristics of α5β1-integrin. A single energy barrier was sufficient to describe the unbinding of both syndecan-4 and decorin from fibronectin, while two barriers were observed for the dissociation of α5β1-integrin from fibronectin. The outer (high affinity) barrier in the interactions of fibronectin with α5β1-integrin and syndecan-4 are characterized by larger barrier heights and widths, and slower dissociation rates than those of the inner (low affinity) barrier in the interactions of fibronectin with α5β1-integrin and decorin. These results indicate that syndecan-4 and (ultimately) α5β1-integrin have the ability to withstand deformation in their interactions with fibronectin, while the decorin-fibronectin interaction is considerably more brittle.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2019 Biophysical Society. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > Department of Physics and Astronomy (Sheffield) |
Funding Information: | Funder Grant number Biotechnology and Biological Sciences Research Council (BBSRC) BB/J009687/1 |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 17 Jul 2019 09:48 |
Last Modified: | 08 Dec 2021 09:35 |
Status: | Published |
Publisher: | Elsevier |
Refereed: | Yes |
Identification Number: | 10.1016/j.bpj.2019.07.002 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:148462 |