Multi-scale thermal stability of a hard thermoplastic protein-based material

Latza, Victoria M.; Guerette, Paul A.; Ding, Dawei; Amini, Shahrouz; Kumar, Akshita; Schmidt, Ingo; Keating, Steven J.; Oxman, Neri; Weaver, James C.; Fratzl, Peter; Miserez, Ali; Mašić, Admir

doi:10.1038/ncomms9313

Cited by 61 publications

(97 citation statements)

References 33 publications

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“…2), as already reported for other structural proteins (33,34). This is of potential interest to controllably deform and reshape the materials on the macroscale, adding increased utility to the solid silk formats.…”

Section: Resultsmentioning

confidence: 53%

Programming function into mechanical forms by directed assembly of silk bulk materials

Marelli

Patel

Duggan

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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We report simple, water-based fabrication methods based on protein self-assembly to generate 3D silk fibroin bulk materials that can be easily hybridized with water-soluble molecules to obtain multiple solid formats with predesigned functions. Controlling self-assembly leads to robust, machinable formats that exhibit thermoplastic behavior consenting material reshaping at the nanoscale, microscale, and macroscale. We illustrate the versatility of the approach by realizing demonstrator devices where large silk monoliths can be generated, polished, and reshaped into functional mechanical components that can be nanopatterned, embed optical function, heated on demand in response to infrared light, or can visualize mechanical failure through colorimetric chemistries embedded in the assembled (bulk) protein matrix. Finally, we show an enzyme-loaded solid mechanical part, illustrating the ability to incorporate biological function within the bulk material with possible utility for sustained release in robust, programmably shapeable mechanical formats.iomimicry draws inspiration from multiple material functions (e.g., antibacterial and antifouling, light manipulation, heat dissipation, water sequestration, superhydrophobicity, adhesiveness, and enhanced mechanical properties) to develop universal fabrication strategies to design new structural materials with utility in a variety of fields ranging from the biomedical, to the technological and architectural. Naturally occurring materials are generated through a bottom-up "generative" process that involves a nontrivial interplay of mechanisms acting across scales from the atomic to the macroscopic. In this context, the assembly of structural biopolymers, the fundamental building blocks of natural materials, leads to hierarchically organized architectures that impart unique functionality to the end material formats.Among the several structural proteins that have been studied, silk fibroin was recently shown to be suited for the generation of a number of biopolymer-based advanced material formats leveraging control of form (through sol-gelsolid transitions) and function (through material modification). The ability to generate functional materials based on water-based silk assembly is predicated on the control of the sol-gel-solid transitions of silk fibroin materials in ambient conditions. In Fig. 1A, the formation of 3D silk fibroin constructs is depicted through its dimensional hierarchy, from the nano-to the macroscales. Silk is extracted from natural sources (i.e., Bombyx mori cocoons) with a previously developed protocol (1) that yields a water suspension of the fibroin protein, where the protein molecules are organized in nanoscopic micelles (or nanoparticles) (top row of Fig. 1A), with an average diameter that changes as a function of concentration and molecular weight (Fig. S1).Control over the dynamics of water evaporation regulates silk-fibroin assembly at the molecular level and the endmaterial format properties. This has been previously observed for natural silk ...

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Section: Resultsmentioning

confidence: 53%

Programming function into mechanical forms by directed assembly of silk bulk materials

Marelli

Patel

Duggan

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…Our recent data on native SRT using SAXS has also revealed a nano-scale assembly of fibrils into a hexagonal lattice. [4] It will be of interest to reconcile this nano-scale arrangement with the peptide secondary structure. Second, Gly-rich modules were not studied in detail in this study since we focused on the modular peptides exhibiting the strongest interactions in the combinatorial assay.…”

Section: Discussionmentioning

confidence: 99%

“…[8] We further refined the selection of peptides based on recent Wide-Angle X-ray Scattering (WAXS) synchrotron experiments of native SRT, which revealed the existence of a network of nano-confined β-sheet structures with dimensions of 2.4-2.6 nm by 3-3.5 8 nm (estimated 5 strands of ~8-10 residues) [4,8] that were arranged isotropically within an amorphous matrix. Based on the β-sheet forming propensities of amino acids and the well-known formation of β-sheets in spider dragline silks arising from poly-Ala sequences, [23] we hypothesized that the combination of Ala-and His-rich domains were the likely source of β strands in the nano-confined β-sheet reinforced polymer network.…”

Section: Peptide Selectionmentioning

confidence: 99%

“…[3] Because of this supramolecular assembly which is stabilized by cooperative weak interactions, SRT exhibit 3 thermoplastic behavior that make them a functional "bioink" for 3D bioprinting applications. [4] It has also been established that recombinant suckerins are versatile building blocks that can be used to engineer various structural and functional materials, including stable colloids, [5] redox-active substrates for the growth of gold nanoparticles, [6] and as hydrogels whose elastic modulus can be modulated over several orders of magnitude. [7] We have previously sequenced dozens of genes encoding members of the suckerin protein family.…”

Section: Introductionmentioning

confidence: 99%

“…[8] The suckerins are highly repetitive and modular, and assemble into a semi-crystalline supramolecular network consisting of an amorphous matrix reinforced with nano-confined β-sheets. [4,8,9] Almost all suckerins consist of peptide motifs that are reminiscent to those found in silk proteins.…”

Section: Introductionmentioning

confidence: 99%

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Modular peptides from the thermoplastic squid sucker ring teeth form amyloid-like cross-β supramolecular networks

et al. 2016

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. (2016). Modular peptides from the thermoplastic squid sucker ring teeth form amyloid-like cross-supramolecular networks. Acta Biomaterialia. https://doi.org/10.1016/j.actbio.2016.09.040Citing this paper Please note that where the full-text provided on King's Research Portal is the Author Accepted Manuscript or Post-Print version this may differ from the final Published version. If citing, it is advised that you check and use the publisher's definitive version for pagination, volume/issue, and date of publication details. And where the final published version is provided on the Research Portal, if citing you are again advised to check the publisher's website for any subsequent corrections. General rightsCopyright and moral rights for the publications made accessible in the Research Portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognize and abide by the legal requirements associated with these rights.•Users may download and print one copy of any publication from the Research Portal for the purpose of private study or research.•You may not further distribute the material or use it for any profit-making activity or commercial gain •You may freely distribute the URL identifying the publication in the Research Portal Take down policy If you believe that this document breaches copyright please contact librarypure@kcl.ac.uk providing details, and we will remove access to the work immediately and investigate your claim. This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. AbstractThe hard sucker ring teeth (SRT) from decapodiforme cephalopods, which are located inside the sucker cups lining the arms and tentacles of these squid species, have recently emerged as a unique model structure for biomimetic structural biopolymers. SRT are entirely composed of modular, block co-polymer-like proteins that self-assemble into a large supramolecular network. In order to unveil the molecular principles behind the SRT's self-assembly and robustness, we describe a combinatorial screening assay that maps the molecular-scale interactions between the most abundant modular peptide blocks of suckerin proteins. By selecting prominent interaction hotspots from this assay, we identified four peptides that exhibited the strongest homo-peptidic interactions, and conducted further in-depth biophysical characterizations complemented by molecular dynamic (MD) simulations to investigate the nature of these interactions. Circular Dichroism (CD) revealed conformations that transitioned from semi-extended poly-proline II (PII) towards β-sheet structure. The peptides s...

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Supramolecular β‐Sheet Suckerin–Based Underwater Adhesives

Deepankumar

Lim

Polte

et al. 2020

Adv Funct Materials

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Nature has evolved several molecular strategies to ensure adhesion in aqueous environments, where artificial adhesives typically fail. One recentlyunveiled molecular design for wet-resistant adhesion is the cohesive cross-β structure characteristic of amyloids, complementing the well-established surface-binding strategy of mussel adhesive proteins based on 3,4-l-dihydroxyphenylalanine (Dopa). Structural proteins that self-assemble into cross β-sheet networks are the suckerins discovered in the sucker ring teeth of squids. Here, light is shed on the wet adhesion of cross-β motifs by producing recombinant suckerin-12, naturally lacking Dopa, and investigating its wet adhesion properties. Surprisingly, the adhesion forces measured on mica reach 70 mN m −1 , exceeding those measured for all mussel adhesive proteins to date. The pressure-sensitive adhesion of artificial suckerins is largely governed by their cross-β motif, as evidenced using control experiments with disrupted cross-β domains that result in complete loss of adhesion. Dopa is also incorporated in suckerin-12 using a residue-specific incorporation strategy that replaces tyrosine with Dopa during expression in Escherichia coli. Although the replacement does not increase the long-term adhesion, it contributes to the initial rapid contact and enhances the adsorption onto model oxide substrates. The findings suggest that suckerins with supramolecular cross-β motifs are promising biopolymers for wet-resistant adhesion.

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Multi-scale thermal stability of a hard thermoplastic protein-based material

Cited by 61 publications

References 33 publications

Programming function into mechanical forms by directed assembly of silk bulk materials

Programming function into mechanical forms by directed assembly of silk bulk materials

Modular peptides from the thermoplastic squid sucker ring teeth form amyloid-like cross-β supramolecular networks

Supramolecular β‐Sheet Suckerin–Based Underwater Adhesives

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