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

Victoria Latza, Paul A. Guerette, Dawei Ding, Shahrouz Amini, Akshita Kumar, Ingo Schmidt, Steven Keating, Neri Oxman, James C. Weaver, Peter Fratzl, Ali Miserez () and Admir Masic ()
Additional contact information
Victoria Latza: Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Potsdam 14424, Germany
Paul A. Guerette: School of Materials Science and Engineering, Nanyang Technological University
Dawei Ding: School of Materials Science and Engineering, Nanyang Technological University
Shahrouz Amini: School of Materials Science and Engineering, Nanyang Technological University
Akshita Kumar: School of Biological Science, Nanyang Technological University
Ingo Schmidt: Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Potsdam 14424, Germany
Steven Keating: MIT Media Lab, Massachusetts Institute of Technology
Neri Oxman: MIT Media Lab, Massachusetts Institute of Technology
James C. Weaver: Wyss Institute for Biologically Inspired Engineering, Harvard University
Peter Fratzl: Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Potsdam 14424, Germany
Ali Miserez: School of Materials Science and Engineering, Nanyang Technological University
Admir Masic: Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Potsdam 14424, Germany

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract 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.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms9313 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9313

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms9313

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().