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Issue 22, 2011
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Revealing the selective interactions of fibronectin with lipid bilayers

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The interaction of extracellular matrix proteins with lipid bilayers is fundamental to cell adhesion and related processes such as tissue formation. In this paper we use atomic force microscopy to examine the interaction between fibronectin and supported lipid bilayers. For binary lipid mixtures that display phase separation, atomic force microscopy shows that fibronectin preferentially and almost exclusively interacts with the gel phase domains, sitting on top of these raised regions. Single molecule force spectroscopy confirms the location of fibronectin on the bilayer and reveals that the mechanical properties of fibronectin are affected by aggregation of the protein on the lipid. We demonstrate that it is possible to measure the thickness of the protein aggregates by identifying a protein layer breakthrough event. Of particular interest are force–distance curves that exhibit a combination of three features, a protein layer breakthrough event, a lipid bilayer breakthrough event, and a sawtooth pattern attributed to fibronectin unfolding. The combination of lipid- and protein-related events on a single force–distance profile, characterizes in detail the lipid/protein interaction. Preferential interactions of fibronectin with lipids suggest that non-specific binding could be important in extracellular matrix protein-cell interactions and that the lateral organization of the cell membrane may play an even greater role in cell adhesion than previously thought.

Graphical abstract: Revealing the selective interactions of fibronectin with lipid bilayers

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Publication details

The article was received on 08 Jul 2011, accepted on 19 Sep 2011 and first published on 12 Oct 2011

Article type: Paper
DOI: 10.1039/C1SM06291C
Soft Matter, 2011,7, 10666-10675

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    Revealing the selective interactions of fibronectin with lipid bilayers

    D. Nordin, O. Yarkoni, N. Savinykh, L. Donlon and D. Frankel, Soft Matter, 2011, 7, 10666
    DOI: 10.1039/C1SM06291C

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