Multi-scale thermal stability of a hard thermoplastic protein-based material
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 properti...
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sg-ntu-dr.10356-805852022-02-16T16:28:41Z Multi-scale thermal stability of a hard thermoplastic protein-based material Latza, Victoria Guerette, Paul Andre Ding, Dawei Amini, Shahrouz Kumar, Akshita Schmidt, Ingo Keating, Steven Oxman, Neri Weaver, James C. Fratzl, Peter Miserez, Ali Masic, Admir School of Materials Science & Engineering School of Biological Sciences Energy Research Institute @ NTU (ERI@N) cephalopod thermal alteration 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 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. NRF (Natl Research Foundation, S’pore) MOE (Min. of Education, S’pore) Published version 2016-05-27T08:55:07Z 2019-12-06T13:52:42Z 2016-05-27T08:55:07Z 2019-12-06T13:52:42Z 2015 Journal Article Latza, 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-. https://hdl.handle.net/10356/80585 http://hdl.handle.net/10220/40580 10.1038/ncomms9313 26387704 Nature Communications © 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 http://creativecommons.org/licenses/by/4.0/ 8 p. application/pdf |
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cephalopod thermal alteration |
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cephalopod thermal alteration Latza, Victoria Guerette, Paul Andre Ding, Dawei Amini, Shahrouz Kumar, Akshita Schmidt, Ingo Keating, Steven Oxman, Neri Weaver, James C. Fratzl, Peter Miserez, Ali Masic, Admir Multi-scale thermal stability of a hard thermoplastic protein-based material |
description |
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 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. |
author2 |
School of Materials Science & Engineering |
author_facet |
School of Materials Science & Engineering Latza, Victoria Guerette, Paul Andre Ding, Dawei Amini, Shahrouz Kumar, Akshita Schmidt, Ingo Keating, Steven Oxman, Neri Weaver, James C. Fratzl, Peter Miserez, Ali Masic, Admir |
format |
Article |
author |
Latza, Victoria Guerette, Paul Andre Ding, Dawei Amini, Shahrouz Kumar, Akshita Schmidt, Ingo Keating, Steven Oxman, Neri Weaver, James C. Fratzl, Peter Miserez, Ali Masic, Admir |
author_sort |
Latza, Victoria |
title |
Multi-scale thermal stability of a hard thermoplastic protein-based material |
title_short |
Multi-scale thermal stability of a hard thermoplastic protein-based material |
title_full |
Multi-scale thermal stability of a hard thermoplastic protein-based material |
title_fullStr |
Multi-scale thermal stability of a hard thermoplastic protein-based material |
title_full_unstemmed |
Multi-scale thermal stability of a hard thermoplastic protein-based material |
title_sort |
multi-scale thermal stability of a hard thermoplastic protein-based material |
publishDate |
2016 |
url |
https://hdl.handle.net/10356/80585 http://hdl.handle.net/10220/40580 |
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1725985538619473920 |