Materials Fabrication from Native and Recombinant Thermoplastic Squid Proteins
Source abstract
Abstract
Natural elastomers made from protein extracts have received significant interest as eco‐friendly functional materials due to their unique mechanical and optical properties emanating from secondary structures. The next generation sequencing approach is used to identify protein sequences in a squid ring teeth complex extracted from Loligo vulgaris and the use of recombinant expression is demonstrated in the fabrication of a new generation of thermoplastic materials. Native and recombinant thermoplastic squid proteins exhibit reversible solid to melt phase transition, enabling them to be thermally shaped into 3D geometries such as fibers, colloids, and thin films. Direct extraction or recombinant expression of protein based thermoplastics opens up new avenues for materials fabrication and synthesis, which will eventually be competitive with the high‐end synthetic oil based plastics.
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Research context
OpenAlex topics: Cephalopods and Marine Biology · Silk-based biomaterials and applications · Biochemical and Structural Characterization
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Materials Research Institute and Department of Engineering Science and Mechanics Pennsylvania State University University Park PA 16802 USA
Department of Chemical Engineering Pennsylvania State University University Park PA 16802 USA
Bioinformatics Consulting Center Pennsylvania State University University Park PA 16802 USA
Huck Institutes of Life Sciences Pennsylvania State University University Park PA 16802 USA
References (31)
Show source-provided references
1. 10.1002/978111867664610.1002/9781118676646 ↗
2. 10.1111/j.1365-313X.2008.03431.x10.1111/j.1365-313X.2008.03431.x ↗
3. 10.1038/nprot.2011.37910.1038/nprot.2011.379 ↗
4. 10.1111/j.1750-3841.2007.00636.x10.1111/j.1750-3841.2007.00636.x ↗
5. 10.1038/nature0238810.1038/nature02388 ↗
6. 10.1002/adma.20120005110.1002/adma.201200051 ↗
7. 10.1016/S1369-7021(12)70091-310.1016/S1369-7021(12)70091-3 ↗
8. 10.1038/nprot.2013.08410.1038/nprot.2013.084 ↗
9. 10.1021/pr060222h10.1021/pr060222h ↗
10. 10.1038/nbt.267110.1038/nbt.2671 ↗
11. Nixon M. · Symp. Zool. Soc. Lond · 1977
12. Williams L. W. · 1910
13. 10.1002/adfm.20140153410.1002/adfm.201401534 ↗
14. 10.1111/j.1469-185X.1972.tb00975.x10.1111/j.1469-185X.1972.tb00975.x ↗
15. 10.1038/nchem.70010.1038/nchem.700 ↗
16. 10.1016/0022-2836(74)90188-010.1016/0022-2836(74)90188-0 ↗
17. 10.1002/pro.556007120510.1002/pro.5560071205 ↗
18. 10.1002/bip.1977.36016060410.1002/bip.1977.360160604 ↗
19. 10.1002/adma.20080119710.1002/adma.200801197 ↗
20. 10.1126/science.107121010.1126/science.1071210 ↗
21. Takajima T. · 1994
22. 10.1016/j.gene.2011.05.02710.1016/j.gene.2011.05.027 ↗
23. 10.1038/nmeth.170110.1038/nmeth.1701 ↗
24. Flory P. J. · 1953
25. 10.1103/PhysRevE.83.05150310.1103/PhysRevE.83.051503 ↗
26. 10.1016/j.foodhyd.2011.08.01610.1016/j.foodhyd.2011.08.016 ↗
27. 10.1016/j.pep.2005.01.01610.1016/j.pep.2005.01.016 ↗
28. 10.1002/adfm.20110301710.1002/adfm.201103017 ↗
29. 10.1038/nmat286410.1038/nmat2864 ↗
30. 10.1088/0022-3727/43/4/04540310.1088/0022-3727/43/4/045403 ↗
31. D. R.Maddison K.‐S.Schulz Internet address:http://tolweb.org2007.