Rising, Anna
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
- Karolinska Institute
Abstract
Spider silk is strong and extensible but still biodegradable and well tolerated when implanted, making it the ultimate biomaterial. Shortcomings that arise in replicating spider silk are due to the use of recombinant spider silk proteins (spidroins) that lack native domains, the use of denaturing conditions under purification and spinning and the fact that the understanding of how spiders control silk formation is incomplete. Recent progress has unraveled the molecular mechanisms of the spidroin N- and C-terminal nonrepetitive domains (NTs and CTs) and revealed the pH and ion gradients in spiders' silk glands, clarifying how spidroin solubility is maintained and how silk is formed in a fraction of a second. Protons and CO2, generated by carbonic anhydrase, affect the stability and structures of the NT and CT in different ways. These insights should allow the design of conditions and devices for the spinning of recombinant spidroins into native-like silk.
Published in
Nature Chemical Biology
2015, volume: 11, number: 5, pages: 309-315
Publisher: NATURE PUBLISHING GROUP
SLU Authors
Johansson, Jan
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
- Karolinska Institute
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
UKÄ Subject classification
Biochemistry
Molecular Biology
Publication identifier
- DOI: https://doi.org/10.1038/NCHEMBIO.1789
Permanent link to this page (URI)
https://res.slu.se/id/publ/68645