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Updated: Jan 21, 2026

Isolation of Chondrocytes and Chondroprogenitors Using Fibronectin Adhesion and Migratory Assay
Published on: October 4, 2024
Distinct Binding Interactions of α5β1-Integrin and Proteoglycans with Fibronectin
Thomas M Kennelly1, Yiran Li2, Yi Cao2
1Department of Physics and Astronomy, University of Sheffield, Sheffield, United Kingdom; Department of Infection, Immunity and Cardiovascular Disease, University of Sheffield, Sheffield, United Kingdom.
Abstract:
Dynamic 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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