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Segmented molecular design of self-healing proteinaceous materials.

Sariola V, Pena-Francesch A, Jung H, Çetinkaya M, Pacheco C, Sitti M, Demirel MC - Sci Rep (2015)

Bottom Line: The hard segments self-assemble into nanoconfined domains to reinforce the material.The healing strength scales sublinearly with contact time, which associates with diffusion and wetting of autohesion.The finding suggests that recombinant structural proteins from heterologous expression have potential as strong and repairable engineering materials.

View Article: PubMed Central - PubMed

Affiliation: Carnegie Mellon University, Department of Mechanical Engineering, Pittsburgh, PA, 15213, USA.

ABSTRACT
Hierarchical assembly of self-healing adhesive proteins creates strong and robust structural and interfacial materials, but understanding of the molecular design and structure-property relationships of structural proteins remains unclear. Elucidating this relationship would allow rational design of next generation genetically engineered self-healing structural proteins. Here we report a general self-healing and -assembly strategy based on a multiphase recombinant protein based material. Segmented structure of the protein shows soft glycine- and tyrosine-rich segments with self-healing capability and hard beta-sheet segments. The soft segments are strongly plasticized by water, lowering the self-healing temperature close to body temperature. The hard segments self-assemble into nanoconfined domains to reinforce the material. The healing strength scales sublinearly with contact time, which associates with diffusion and wetting of autohesion. The finding suggests that recombinant structural proteins from heterologous expression have potential as strong and repairable engineering materials.

No MeSH data available.


Related in: MedlinePlus

Sequencing and heterologous expression of the self-healing thermoplastic squid ring teeth protein.(A) Schematic of supramolecular self-assembly. (B) The amino acid sequence of the protein showing a segmented copolymer structure. The single letter amino acid abbreviations follow the standard convention. Self-assembling β-sheet regions are colored green and amorphous regions red. (C) The 18 kDa recombinant protein powder is obtained using next generation sequencing and heterologous expression. (D,E) The recombinant protein dissolves in polar solvents (D) and can be cast into various shapes (E). The material self-assembles upon solvent evaporation. (F) Dog bone shaped recombinant protein beam after cutting in half. (G) The beam after pressing together in warm 45 °C water.
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f1: Sequencing and heterologous expression of the self-healing thermoplastic squid ring teeth protein.(A) Schematic of supramolecular self-assembly. (B) The amino acid sequence of the protein showing a segmented copolymer structure. The single letter amino acid abbreviations follow the standard convention. Self-assembling β-sheet regions are colored green and amorphous regions red. (C) The 18 kDa recombinant protein powder is obtained using next generation sequencing and heterologous expression. (D,E) The recombinant protein dissolves in polar solvents (D) and can be cast into various shapes (E). The material self-assembles upon solvent evaporation. (F) Dog bone shaped recombinant protein beam after cutting in half. (G) The beam after pressing together in warm 45 °C water.

Mentions: Underwater self-healing materials can be found in nature11, and significant research efforts have focused on mimicking the interfacial chemistry of marine barnacles1213. Yet self-healing proteins are also known to self-assemble through supramolecular organization and the understanding of the role of this supramolecular self-assembly in the self-healing process remains limited. We propose that Nature uses this supramolecular self-assembly to achieve stiff self-healing structural proteins with soft/hard domain separation (Fig. 1A).


Segmented molecular design of self-healing proteinaceous materials.

Sariola V, Pena-Francesch A, Jung H, Çetinkaya M, Pacheco C, Sitti M, Demirel MC - Sci Rep (2015)

Sequencing and heterologous expression of the self-healing thermoplastic squid ring teeth protein.(A) Schematic of supramolecular self-assembly. (B) The amino acid sequence of the protein showing a segmented copolymer structure. The single letter amino acid abbreviations follow the standard convention. Self-assembling β-sheet regions are colored green and amorphous regions red. (C) The 18 kDa recombinant protein powder is obtained using next generation sequencing and heterologous expression. (D,E) The recombinant protein dissolves in polar solvents (D) and can be cast into various shapes (E). The material self-assembles upon solvent evaporation. (F) Dog bone shaped recombinant protein beam after cutting in half. (G) The beam after pressing together in warm 45 °C water.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4555047&req=5

f1: Sequencing and heterologous expression of the self-healing thermoplastic squid ring teeth protein.(A) Schematic of supramolecular self-assembly. (B) The amino acid sequence of the protein showing a segmented copolymer structure. The single letter amino acid abbreviations follow the standard convention. Self-assembling β-sheet regions are colored green and amorphous regions red. (C) The 18 kDa recombinant protein powder is obtained using next generation sequencing and heterologous expression. (D,E) The recombinant protein dissolves in polar solvents (D) and can be cast into various shapes (E). The material self-assembles upon solvent evaporation. (F) Dog bone shaped recombinant protein beam after cutting in half. (G) The beam after pressing together in warm 45 °C water.
Mentions: Underwater self-healing materials can be found in nature11, and significant research efforts have focused on mimicking the interfacial chemistry of marine barnacles1213. Yet self-healing proteins are also known to self-assemble through supramolecular organization and the understanding of the role of this supramolecular self-assembly in the self-healing process remains limited. We propose that Nature uses this supramolecular self-assembly to achieve stiff self-healing structural proteins with soft/hard domain separation (Fig. 1A).

Bottom Line: The hard segments self-assemble into nanoconfined domains to reinforce the material.The healing strength scales sublinearly with contact time, which associates with diffusion and wetting of autohesion.The finding suggests that recombinant structural proteins from heterologous expression have potential as strong and repairable engineering materials.

View Article: PubMed Central - PubMed

Affiliation: Carnegie Mellon University, Department of Mechanical Engineering, Pittsburgh, PA, 15213, USA.

ABSTRACT
Hierarchical assembly of self-healing adhesive proteins creates strong and robust structural and interfacial materials, but understanding of the molecular design and structure-property relationships of structural proteins remains unclear. Elucidating this relationship would allow rational design of next generation genetically engineered self-healing structural proteins. Here we report a general self-healing and -assembly strategy based on a multiphase recombinant protein based material. Segmented structure of the protein shows soft glycine- and tyrosine-rich segments with self-healing capability and hard beta-sheet segments. The soft segments are strongly plasticized by water, lowering the self-healing temperature close to body temperature. The hard segments self-assemble into nanoconfined domains to reinforce the material. The healing strength scales sublinearly with contact time, which associates with diffusion and wetting of autohesion. The finding suggests that recombinant structural proteins from heterologous expression have potential as strong and repairable engineering materials.

No MeSH data available.


Related in: MedlinePlus