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

Multi-scale thermal stability of a hard thermoplastic protein-based material.
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DOI:
10.1038/ncomms9313
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发表时间:
2015-09-21
影响因子:
16.6
通讯作者:
Masic A
Masic A
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Latza V;Guerette PA;Ding D;Amini S;Kumar A;Schmidt I;Keating S;Oxman N;Weaver JC;Fratzl P;Miserez A;Masic A

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Although thermoplastic materials are mostly derived from petro-chemicals, it would be highly desirable, from a sustainability perspective, to produce them instead from renewable biopolymers. Unfortunately, biopolymers exhibiting thermoplastic behaviour and which preserve their mechanical properties post processing are essentially non-existent. The robust sucker ring teeth (SRT) from squid and cuttlefish are one notable exception of thermoplastic biopolymers. Here we describe thermoplastic processing of squid SRT via hot extrusion of fibres, demonstrating the potential suitability of these materials for large-scale thermal forming. Using high-resolution in situ X-ray diffraction and vibrational spectroscopy, we elucidate the molecular and nanoscale features responsible for this behaviour and show that SRT consist of semi-crystalline polymers, whereby heat-resistant, nanocrystalline β-sheets embedded within an amorphous matrix are organized into a hexagonally packed nanofibrillar lattice. This study provides key insights for the molecular design of biomimetic protein- and peptide-based thermoplastic structural biopolymers with potential biomedical and 3D printing applications. Sucker ring teeth from squid and cuttlefish represent rare examples of thermoplastic biopolymers. Here, the authors demonstrate how these materials may be processed for implementation in biomedical and 3D printing applications.