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Spider wrapping silk fibre architecture arising from its modular soluble protein precursor.
- Source :
-
Scientific reports [Sci Rep] 2015 Jun 26; Vol. 5, pp. 11502. Date of Electronic Publication: 2015 Jun 26. - Publication Year :
- 2015
-
Abstract
- Spiders store spidroins in their silk glands as high concentration aqueous solutions, spinning these dopes into fibres with outstanding mechanical properties. Aciniform (or wrapping) silk is the toughest spider silk and is devoid of the short amino acid sequence motifs characteristic of the other spidroins. Using solution-state NMR spectroscopy, we demonstrate that the 200 amino acid Argiope trifasciata AcSp1 repeat unit contrasts with previously characterized spidroins, adopting a globular 5-helix bundle flanked by intrinsically disordered N- and C-terminal tails. Split-intein-mediated segmental NMR-active isotope-enrichment allowed unambiguous demonstration of modular and malleable "beads-on-a-string" concatemeric behaviour. Concatemers form fibres upon manual drawing with silk-like morphology and mechanical properties, alongside secondary structuring and orientation consistent with native AcSp1 fibres. AcSp1 structural stability varies locally, with the fifth helix denaturing most readily. The structural transition of aciniform spidroin from a mostly α-helical dope to a mixed α-helix/β-sheet-containing fibre can be directly related to spidroin architecture and stability.
- Subjects :
- Amino Acid Motifs
Animals
Dynamic Light Scattering
Fibroins chemistry
Hydrodynamics
Insect Proteins chemistry
Insect Proteins genetics
Insect Proteins metabolism
Nuclear Magnetic Resonance, Biomolecular
Protein Precursors metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Fusion Proteins biosynthesis
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Protein Precursors chemistry
Silk chemistry
Spiders metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 5
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 26112753
- Full Text :
- https://doi.org/10.1038/srep11502