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Search: AMNE:(MEDICAL AND HEALTH SCIENCES Medical Biotechnology Biomaterials Science) > (2020-2024) > Tyrosine residues m...

  • Greco, Gabriele (author)

Tyrosine residues mediate supercontraction in biomimetic spider silk

  • Article/chapterEnglish2021

Publisher, publication year, extent ...

  • 2021-04-12
  • Springer Science and Business Media LLC,2021
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:su-193037
  • https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-193037URI
  • https://doi.org/10.1038/s43246-021-00147-wDOI
  • https://res.slu.se/id/publ/114644URI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Exposing spider silk to wet conditions can cause supercontraction. Here, tyrosine amino acid residues within the amorphous regions are found to contribute to supercontraction, which can be controlled by protein engineering. Water and humidity severely affect the material properties of spider major ampullate silk, causing the fiber to become plasticized, contract, swell and undergo torsion. Several amino acid residue types have been proposed to be involved in this process, but the complex composition of the native fiber complicates detailed investigations. Here, we observe supercontraction in biomimetically produced artificial spider silk fibers composed of defined proteins. We found experimental evidence that proline is not the sole residue responsible for supercontraction and that tyrosine residues in the amorphous regions of the silk fiber play an important role. Furthermore, we show that the response of artificial silk fibers to humidity can be tuned, which is important for the development of materials for applications in wet environments, eg producing water resistant fibers with maximal strain at break and toughness modulus.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Arndt, Tina (author)
  • Schmuck, BenjaminKarolinska Institute(Swepub:slu)97577 (author)
  • Francis, Juanita (author)
  • Bäcklund, Fredrik G. (author)
  • Shilkova, Olga (author)
  • Barth, AndreasStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)abart (author)
  • Gonska, NathalieSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för anatomi, fysiologi och biokemi,Department of Anatomy, Physiology and Biochemistry (AFB) (author)
  • Seisenbaeva, GulaimSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences(Swepub:slu)47225 (author)
  • Kessler, VadimSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences(Swepub:slu)46900 (author)
  • Johansson, Jan (author)
  • Pugno, Nicola M. (author)
  • Rising, AnnaSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för anatomi, fysiologi och biokemi,Department of Anatomy, Physiology and Biochemistry (AFB),Karolinska Institute(Swepub:slu)47422 (author)
  • Karolinska InstituteInstitutionen för biokemi och biofysik (creator_code:org_t)
  • Sveriges lantbruksuniversitet

Related titles

  • In:Communications materials: Springer Science and Business Media LLC2:12662-4443

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