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Folding driven self-assembly of a stimuli-responsive peptide-hyaluronan hybrid hydrogel.

ABSTRACT: Protein-metal ion interactions are ubiquitous in nature and can be utilized for controlling the self-assembly of complex supramolecular architectures and materials. Here, a tunable supramolecular hydrogel is described, obtained by self-assembly of a Zn2+-responsive peptide-hyaluronic acid hybrid synthesized using strain promoted click chemistry. Addition of Zn2+ triggers folding of the peptides into a helix-loop-helix motif and dimerization into four-helix bundles, resulting in hydrogelation. Removal of the Zn2+ by chelators results in rapid hydrogel disassembly. Degradation of the hydrogels can also be time-programed by encapsulation of a hydrolyzing enzyme within the gel, offering multiple possibilities for modulating materials properties and release of encapsulated species. The hydrogel further shows potential antioxidant properties when evaluated using an in vitro model for reactive oxygen species.

SUBMITTER: Selegard R

PROVIDER: S-EPMC5539109 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Folding driven self-assembly of a stimuli-responsive peptide-hyaluronan hybrid hydrogel.

Selegård Robert R Aronsson Christopher C Brommesson Caroline C Dånmark Staffan S Aili Daniel D

Scientific reports 20170801 1

Protein-metal ion interactions are ubiquitous in nature and can be utilized for controlling the self-assembly of complex supramolecular architectures and materials. Here, a tunable supramolecular hydrogel is described, obtained by self-assembly of a Zn<sup>2+</sup>-responsive peptide-hyaluronic acid hybrid synthesized using strain promoted click chemistry. Addition of Zn<sup>2+</sup> triggers folding of the peptides into a helix-loop-helix motif and dimerization into four-helix bundles, resultin ...[more]

PMID: 28765593

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