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Mechanotransductive surfaces for reversible biocatalysis activation

Nature Materials volume 8, pages 731–735 (2009)Cite this article

Abstract

Fibronectin, like other proteins involved in mechanotransduction, has the ability to exhibit recognition sites under mechanical stretch1,2,3. Such cryptic sites are buried inside the protein structure in the native fold and become exposed under an applied force4, thereby activating specific signalling pathways5. Here, we report the design of new active polymeric nanoassembled surfaces that show some similarities to these cryptic sites. These nanoassemblies consist of a first polyelectrolyte multilayer6 stratum loaded with enzymes and capped with a second polyelectrolyte multilayer acting as a mechanically sensitive nanobarrier. The biocatalytic activity of the film is switched on/off reversibly by mechanical stretching, which exposes enzymes through the capping barrier, similarly to mechanisms involved in proteins during mechanotransduction. This first example of a new class of biologically inspired surfaces should have great potential in the design of various devices aimed to trigger and modulate chemical reactions by mechanical action with applications in the field of microfluidic devices or mechanically controlled biopatches for example.

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Figure 1: Triggering of biocatalytic activity of reservoir/barrier films induced by mechanical stretching.
Figure 2: Scheme illustrating the mechanism involved in the mechanically sensitive biocatalytic coating.
Figure 3: Triggering of biocatalytic activity of reservoir/barrier films induced by mechanical stretching for three different nanosized barrier thicknesses.
Figure 4: Reversible biocatalytic activation (on/off states) achieved through stretched/unstretched cycles on a reservoir/barrier film.

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Acknowledgements

Confocal microscopy was carried out in Strasbourg Esplanade Cellular Imaging Facility, funded by CNRS, INSERM, Louis Pasteur University and Alsace Region. We thank K. Benmlih for the build-up of the stretching devices and we are grateful to S. Lesko (Veeco, Dourdan, France) for helping with AFM experiments, D. Vautier and J. H. Lignot for fruitful discussions about immunogold detection, C. Ringwald for designing silicon cells and C. Bouthier for her assistance. We acknowledge support from the Région Alsace for financial contribution to the AFM equipment and P.S. thanks COST D43 for financial support.

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Authors and Affiliations

  1. Institut National de la Santé et de la Recherche Médicale, INSERM Unité 977, ‘Biomaterials and Tissue Engineering’, 11 rue Humann, 67085 Strasbourg Cedex, France

    Damien Mertz, Cédric Vogt, Joseph Hemmerlé, Vincent Ball, Jean-Claude Voegel & Philippe Lavalle

  2. Faculté de Chirurgie Dentaire, Université de Strasbourg, 1 Place de l’Hôpital, 67000 Strasbourg, France

    Damien Mertz, Cédric Vogt, Joseph Hemmerlé, Vincent Ball, Jean-Claude Voegel & Philippe Lavalle

  3. Centre National de la Recherche Scientifique, UPR22, Institut Charles Sadron, 23 rue du Loess, BP 84047, 67034 Strasbourg, Cedex 2, France

    Damien Mertz, Cédric Vogt & Pierre Schaaf

  4. Centre National de la Recherche Scientifique, UPR2357, Institut de Biologie Moléculaire des Plantes, 12, rue du Général Zimmer, 67084 Strasbourg Cedex, France

    Jérôme Mutterer

  5. Hôpitaux Universitaires de Strasbourg, 1 Place de l’Hôpital, 67000 Strasbourg, France

    Philippe Lavalle

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  1. Damien Mertz
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  4. Jérôme Mutterer
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  5. Vincent Ball
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  6. Jean-Claude Voegel
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  7. Pierre Schaaf
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Contributions

D.M., P.L. and C.V. carried out the experiments. P.S. and P.L. brought-up the concept. P.S. P.L. and J.C.V. designed the experiments. J.H. designed the experimental set-up. D.M., J.M. and C.V. analysed the data. V.B. proposed the adapted enzymatic model. P.S. and P.L. co-wrote the paper.

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Correspondence to Jean-Claude Voegel.

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Mertz, D., Vogt, C., Hemmerlé, J. et al. Mechanotransductive surfaces for reversible biocatalysis activation. Nature Mater 8, 731–735 (2009). https://doi.org/10.1038/nmat2504

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