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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Main Authors: 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
Other Authors: School of Materials Science & Engineering
Format: Article
Published: 2016
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Online Access:https://hdl.handle.net/10356/80585
http://hdl.handle.net/10220/40580
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Institution: Nanyang Technological University
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spelling 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
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
topic cephalopod
thermal alteration
spellingShingle 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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