Greco, Gabriele
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
- University of Trento
Research article2022Peer reviewedOpen access
Arndt, Tina; Greco, Gabriele; Schmuck, Benjamin; Bunz, Jessica; Shilkova, Olga; Francis, Juanita; Pugno, Nicola M.; Jaudzems, Kristaps; Barth, Andreas; Johansson, Jan; Rising, Anna
Spider silk is the toughest fiber found in nature, and bulk production of artificial spider silk that matches its mechanical properties remains elusive. Development of miniature spider silk proteins (mini-spidroins) has made large-scale fiber production economically feasible, but the fibers' mechanical properties are inferior to native silk. The spider silk fiber's tensile strength is conferred by poly-alanine stretches that are zipped together by tight side chain packing in beta-sheet crystals. Spidroins are secreted so they must be void of long stretches of hydrophobic residues, since such segments get inserted into the endoplasmic reticulum membrane. At the same time, hydrophobic residues have high beta-strand propensity and can mediate tight inter-beta-sheet interactions, features that are attractive for generation of strong artificial silks. Protein production in prokaryotes can circumvent biological laws that spiders, being eukaryotic organisms, must obey, and the authors thus design mini-spidroins that are predicted to more avidly form stronger beta-sheets than the wildtype protein. Biomimetic spinning of the engineered mini-spidroins indeed results in fibers with increased tensile strength and two fiber types display toughness equal to native dragline silks. Bioreactor expression and purification result in a protein yield of approximate to 9 g L-1 which is in line with requirements for economically feasible bulk scale production.
biomimetic materials; biomimetic spider silk fibers; fibers; protein engineering; recombinant protein production
Advanced Functional Materials
2022, Volume: 32, number: 23, article number: 2200986Publisher: WILEY-V C H VERLAG GMBH
Bio Materials
Biochemistry and Molecular Biology
DOI: https://doi.org/10.1002/adfm.202200986
https://res.slu.se/id/publ/116646