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Protein-induced low molecular weight hydrogelator self-assembly through a self-sustaining process

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Abstract

Controlling how, when and where a self-assembly process occurs is essential for the design of the next generation of smart materials. Along this route, enzyme-assisted self-assembly is a powerful tool developed during the last decade. Here we introduce another strategy allowing for spatiotemporal control over peptide self-assemblies. We use a Fmoc-peptide precursor in dynamic equilibrium with its low molecular weight hydrogelator (LMWH) through a reversible disulfide bond. In the absence of proteins, no self-assembly of the hydrogelator is observed. In the presence of proteins, their interactions with the precursor initiate a self-assembly process of the hydrogelator around them. This self-assembly displaces the equilibrium between precursor and LMWH according to Le Chatelier's principle, producing new hydrogelators available to pursue the self-assembly growth. One thus establishes a self-sustaining cycle fuelled by the self-assembly itself until full consumption of the LMWH. For proteins in solutions this process can lead to a supramolecular hydrogel whereas for proteins deposited on a surface, the gel growth is initiated exclusively from the surface.

Graphical abstract: Protein-induced low molecular weight hydrogelator self-assembly through a self-sustaining process

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Publication details

The article was received on 19 Jan 2019, accepted on 07 Mar 2019 and first published on 11 Mar 2019


Article type: Edge Article
DOI: 10.1039/C9SC00312F
Citation: Chem. Sci., 2019, Advance Article
  • Open access: Creative Commons BY-NC license
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    Protein-induced low molecular weight hydrogelator self-assembly through a self-sustaining process

    J. Rodon Fores, M. Criado-Gonzalez, M. Schmutz, C. Blanck, P. Schaaf, F. Boulmedais and L. Jierry, Chem. Sci., 2019, Advance Article , DOI: 10.1039/C9SC00312F

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