Structural and Mechanical Roles for the C-Terminal Nonrepetitive Domain Become Apparent in Recombinant Spider Aciniform Silk

Lingling Xu, Thierry Lefèvre, Kathleen E. Orrell, Qing Meng, Michèle Auger, Xiang Qin Liu, Jan K. Rainey

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

Spider aciniform (or wrapping) silk is the toughest of the seven types of spider silks/glue due to a combination of high elasticity and strength. Like most spider silk proteins (spidroins), aciniform spidroin (AcSp1) has a large core repetitive domain flanked by relatively short N- and C-terminal nonrepetitive domains (the NTD and CTD, respectively). The major ampullate silk protein (MaSp) CTD has been shown to control protein solubility and fiber formation, but the aciniform CTD function remains unknown. Here, we compare fiber mechanical properties, solution-state structuring, and fibrous state secondary structural composition, and orientation relative to native aciniform silk for two AcSp1 repeat units with or without fused AcSp1- and MaSp-derived CTDs alongside three AcSp1 repeat units without a CTD. The native AcSp1 CTD uniquely modulated fiber mechanical properties, relative to all other constructs, directly correlating to a native-like structural transformation and alignment.

Original languageEnglish
Pages (from-to)3678-3686
Number of pages9
JournalBiomacromolecules
Volume18
Issue number11
DOIs
Publication statusPublished - Nov 13 2017

Bibliographical note

Funding Information:
Thanks to Prof. Michel Peźolet for helpful discussions during the early stages of this work; Dr. Mike Lumsden (NMR3 Facility, Dalhousie University) and Ian Burton (National Research Council (NRC), Halifax NS) for NMR instrument support; Bruce Stewart for technical assistance; Dr. David Waisman for CD spectropolarimeter access; Patricia Scallion for SEM assistance; and Jingna Zhao for tensile testing assistance. This work was supported by Discovery Grants from the Natural Sciences and Engineering Research Council of Canada (NSERC, to M.A., X.-Q.L., and J.K.R.); Dalhousie Medical Research Foundation Capital Equipment Grants (to X.-Q.L. and J.K.R.); an NSERC Research Tools & Instruments Grant (to J.K.R.); an NSERC Discovery Accelerator Supplement (to J.K.R.); the National Natural Science Foundation of China (No. 31570721 to Q.M.); the Science and Technology Commission of Shanghai Municipality (Nos. 14521100700 and 14520720200 to Q.M.); the Regroupement queb́ ećois de recherche sur la fonction, l’ingeńierie et les applications des proteínes (PROTEO), the Centre de recherche sur les mateŕ iaux avanceś (CERMA) and the Centre queb́ ećois sur les mateŕ iaux fonctionnels (CQMF) (to M.A.); a Canadian Institutes for Health Research New Investigator Award (to J.K.R.); and an NSERC Undergraduate Student Research Award (to K.E.O.). The TCI probe for the 16.4 T NMR spectrometer at the NRC was provided by Dalhousie University through an Atlantic Canada Opportunities Agency Grant.

Publisher Copyright:
© 2017 American Chemical Society.

ASJC Scopus Subject Areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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Xu, L., Lefèvre, T., Orrell, K. E., Meng, Q., Auger, M., Liu, X. Q., & Rainey, J. K. (2017). Structural and Mechanical Roles for the C-Terminal Nonrepetitive Domain Become Apparent in Recombinant Spider Aciniform Silk. Biomacromolecules, 18(11), 3678-3686. https://doi.org/10.1021/acs.biomac.7b01057