Cao Y

Geoghegan M

Kennelly TM

Li Y

Qwarnstrom EE

\ua9 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

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Distinct Binding Interactions of α5<em>β</em>1-Integrin and Proteoglycans with Fibronectin

https://eprint.ncl.ac.uk/fulltext.aspx?url=262402/D0EB159E-72CF-4041-B29A-2388963A18BD.pdf&pub_id=262402

Distinct Binding Interactions of α5<em>β</em>1-Integrin and Proteoglycans with Fibronectin

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