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Article Dans Une Revue Nature Materials Année : 2009

Mechanotransductive surfaces for reversible biocatalysis activation

Résumé

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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Dates et versions

hal-00430843 , version 1 (10-11-2009)

Identifiants

  • HAL Id : hal-00430843 , version 1

Citer

D. Mertz, C. Vogt, J. Hemmerle, J. Mutterer, V. Ball, et al.. Mechanotransductive surfaces for reversible biocatalysis activation. Nature Materials, 2009, 8 (9), pp.731-735. ⟨hal-00430843⟩
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