Engineering shape memory and morphing protein hydrogels based on protein unfolding and folding

Engineering shape memory/morphing materials have achieved considerable progress in polymer-based systems with broad potential applications. However, engineering protein-based shape memory/morphing materials remains challenging and under-explored. Here we report the design of a bilayer protein-based...

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Veröffentlicht in:Nature communications 2022-01, Vol.13 (1), p.137-137, Article 137
Hauptverfasser: Bian, Qingyuan, Fu, Linglan, Li, Hongbin
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Sprache:eng
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Zusammenfassung:Engineering shape memory/morphing materials have achieved considerable progress in polymer-based systems with broad potential applications. However, engineering protein-based shape memory/morphing materials remains challenging and under-explored. Here we report the design of a bilayer protein-based shape memory/morphing hydrogel based on protein folding-unfolding mechanism. We fabricate the protein-bilayer structure using two tandem modular elastomeric proteins (GB1) 8 and (FL) 8 . Both protein layers display distinct denaturant-dependent swelling profiles and Young’s moduli. Due to such protein unfolding-folding induced changes in swelling, the bilayer hydrogels display highly tunable and reversible bidirectional bending deformation depending upon the denaturant concentration and layer geometry. Based on these programmable and reversible bending behaviors, we further utilize the protein-bilayer structure as hinge to realize one-dimensional to two-dimensional and two-dimensional to three-dimensional folding transformations of patterned hydrogels. The present work will offer new inspirations for the design and fabrication of novel shape morphing materials. Engineering shape memory and morphing materials achieved considerable progress in polymer-based systems, but protein-based shape memory and morphing materials remain less investigated. Here, the authors report the engineering of protein-based shape memory and morphing hydrogels using protein folding-unfolding as a general mechanism to trigger shape morphing in protein-bilayer structures.
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-021-27744-0