Issue 22, 2012

Characterising single fibronectin–integrin complexes

Abstract

In this paper, single complexes of individual fibronectin molecules bound to integrin proteins were studied using atomic force microscopy (AFM). It was found that the fibronectin binds to the head region of the flat lying molecule when the integrins are adsorbed onto mica. Confirmation that fibronectin is bound was via single molecule force spectroscopy and loading rate analysis. Incorporation of the integrin into a supported lipid bilayer stabilizes the integrin in terms of its orientation. The head region of the integrin was shown to remain functional allowing single fibronectin molecules to interact with the head region protruding from the lipid bilayer surface. In addition the integrins were found to selectively partition into the gel phase DPPC domains, an observation consistent with the lipid raft hypothesis. Although a supported lipid bilayer will perturb the dynamic study of transmembrane proteins, this work demonstrates that integrins stabilized in this manner are functional and available for the study of biomolecular interactions.

Graphical abstract: Characterising single fibronectin–integrin complexes

Supplementary files

Article information

Article type
Paper
Submitted
14 Nov 2011
Accepted
23 Apr 2012
First published
01 May 2012

Soft Matter, 2012,8, 6151-6160

Characterising single fibronectin–integrin complexes

D. Nordin, L. Donlon and D. Frankel, Soft Matter, 2012, 8, 6151 DOI: 10.1039/C2SM07171A

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