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Lookup NU author(s): Professor Mark GeogheganORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2019 Biophysical SocietyDynamic single-molecule force spectroscopy was performed to monitor the unbinding of fibronectin with the proteoglycans syndecan-4 (SDC4) 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 SDC4 and decorin from fibronectin, whereas two barriers were observed for the dissociation of α5β1-integrin from fibronectin. The outer (high-affinity) barriers in the interactions of fibronectin with α5β1-integrin and SDC4 are characterized by larger barrier heights and widths and slower dissociation rates than those of the inner (low-affinity) barriers in the interactions of fibronectin with α5β1-integrin and decorin. These results indicate that SDC4 and (ultimately) α5β1-integrin have the ability to withstand deformation in their interactions with fibronectin, whereas the decorin-fibronectin interaction is considerably more brittle.
Author(s): Kennelly TM, Li Y, Cao Y, Qwarnstrom EE, Geoghegan M
Publication type: Article
Publication status: Published
Journal: Biophysical Journal
Year: 2019
Volume: 117
Issue: 4
Pages: 688-695
Print publication date: 20/08/2019
Online publication date: 05/07/2019
Acceptance date: 03/07/2019
Date deposited: 19/12/2019
ISSN (print): 0006-3495
ISSN (electronic): 1542-0086
Publisher: Biophysical Society
URL: https://doi.org/10.1016/j.bpj.2019.07.002
DOI: 10.1016/j.bpj.2019.07.002
PubMed id: 31337547
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