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Disulfide crosslinking and helical coiling of peptide micelles facilitate the formation of a printable hydrogel

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Abstract

We report that the helical coiling of micelles induced by disulfide crosslinking in a lyotropic peptide liquid crystal leads to the formation of a printable hydrogel. The (9-fluorenylmethyloxycarbonyl)-protected phenylalanine–phenylalanine–cysteine tripeptide could firstly self-assemble into aligned micelles at high pH values via noncovalent interactions, leading to the formation of a viscous solution. Intriguingly, the cross-linking of the sulfhydryl group between the peptides changed greatly the rheological properties of the peptide solutions, leading to a 6500-fold increase of the storage modulus to 39 kPa. This led to the formation of a self-supporting peptide hydrogel with a series of improved physical properties, including shear-thinning and thixotropy. The formation of the peptide hydrogels with enhanced physical properties can be attributed to the structural transition of the parallelly aligned worm-like micelles into coiled nanohelices induced by the cross-linking of disulfide bonding. The findings deepen our understanding on the relationship between micelle chirality and gel properties, and provide a strategy to fabricate highly functional materials via simultaneous noncovalent and covalent polymerizations.

Graphical abstract: Disulfide crosslinking and helical coiling of peptide micelles facilitate the formation of a printable hydrogel

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Publication details

The article was received on 27 Nov 2018, accepted on 24 Mar 2019 and first published on 25 Mar 2019


Article type: Paper
DOI: 10.1039/C8TB03121E
Citation: J. Mater. Chem. B, 2019, Advance Article

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    Disulfide crosslinking and helical coiling of peptide micelles facilitate the formation of a printable hydrogel

    X. Yang, Y. Wang, W. Qi, R. Xing, X. Yang, Q. Xing, R. Su and Z. He, J. Mater. Chem. B, 2019, Advance Article , DOI: 10.1039/C8TB03121E

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