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dc.contributor.authorLatza, Victoriaen
dc.contributor.authorGuerette, Paul Andreen
dc.contributor.authorDing, Daweien
dc.contributor.authorAmini, Shahrouzen
dc.contributor.authorKumar, Akshitaen
dc.contributor.authorSchmidt, Ingoen
dc.contributor.authorKeating, Stevenen
dc.contributor.authorOxman, Nerien
dc.contributor.authorWeaver, James C.en
dc.contributor.authorFratzl, Peteren
dc.contributor.authorMiserez, Alien
dc.contributor.authorMasic, Admiren
dc.identifier.citationLatza, V., Guerette, P. A., Ding, D., Amini, S., Kumar, A., Schmidt, I., et al. (2015). Multi-scale thermal stability of a hard thermoplastic protein-based material. Nature Communications, 6, 8313-.en
dc.description.abstractAlthough 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 b-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.en
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.format.extent8 p.en
dc.relation.ispartofseriesNature Communicationsen
dc.rights© 2015 This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
dc.subjectthermal alterationen
dc.titleMulti-scale thermal stability of a hard thermoplastic protein-based materialen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Materials Science & Engineeringen
dc.contributor.schoolSchool of Biological Sciencesen
dc.contributor.researchEnergy Research Institute @ NTU (ERI@N)en
dc.description.versionPublished versionen
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