Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy

Sammanfattning

Biomimetic spinning of artificial spider silk requires that the terminal domains of designed minispidroins undergo specific structural changes in concert with the beta-sheet conversion of the repetitive region. Herein, we combine solution and solid-state NMR methods to probe domain-specific structural changes in the NT2RepCT minispidroin, which allows us to assess the degree of biomimicry of artificial silk spinning. In addition, we show that the structural effects of post-spinning procedures can be examined. By studying the impact of NT2RepCT fiber drying, we observed a reversible beta-to-alpha conversion. We think that this approach will be useful for guiding the optimization of artificial spider silk fibers.

Nyckelord

biomimicry; fibrous proteins; NMR spectroscopy; spider silk

Publicerad i

Angewandte Chemie International Edition
2017, volym: 56, nummer: 41, sidor: 12571-12575
Utgivare: WILEY-V C H VERLAG GMBH

SLU författare

• Andersson, Marlene

  • Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
    

• Nordling, Kerstin

  • Karolinska institutet

• Johansson, Jan

  • Karolinska institutet

• Rising, Anna

  • Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Molekylärbiologi
Biokemi

Publikationens identifierare

• DOI: https://doi.org/10.1002/anie.201706649

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/90937