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Issue 38, 2012
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Complete unfolding of fibronectin reveals surface interactions

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Abstract

Surface interactions between proteins and biomaterials are fundamental to biological processes and a means to measure these interactions with minimum perturbation to the system of interest has remained elusive. In this paper we address this problem by analysing the total unfolding force of a surface adsorbed protein, in this case fibronectin. By summing all unfolding events, domains that may be interacting with the surface are considered. We propose a protocol for comparing like with like in terms of protein behaviour based on the number of events in the sawtooth pattern. Using this method it is possible to distinguish surface behaviour between several biologically relevant surfaces including hydroxyapatite, collagen and lipids. Moreover the difference in total unfolding confirms the difference in protein interaction/conformation on the various surfaces.

Graphical abstract: Complete unfolding of fibronectin reveals surface interactions

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Publication details

The article was received on 06 Jun 2012, accepted on 07 Aug 2012 and first published on 17 Aug 2012


Article type: Paper
DOI: 10.1039/C2SM26315G
Citation: Soft Matter, 2012,8, 9933-9940
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    Complete unfolding of fibronectin reveals surface interactions

    L. Donlon, D. Nordin and D. Frankel, Soft Matter, 2012, 8, 9933
    DOI: 10.1039/C2SM26315G

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