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Structural Diversity of Native Major Ampullate, Minor Ampullate, Cylindriform, and Flagelliform Silk Proteins in Solution

Greving, Imke ; Terry, Ann E. LU ; Holland, Chris ; Boulet-Audet, Maxime ; Grillo, Isabelle ; Vollrath, Fritz and Dicko, Cedric LU orcid (2020) In Biomacromolecules 21(8). p.3387-3393
Abstract

The foundations of silk spinning, the structure, storage, and activation of silk proteins, remain highly debated. By combining solution small-angle neutron and X-ray scattering (SANS and SAXS) alongside circular dichroism (CD), we reveal a shape anisotropy of the four principal native spider silk feedstocks from Nephila edulis. We show that these proteins behave in solution like elongated semiflexible polymers with locally rigid sections. We demonstrated that minor ampullate and cylindriform proteins adopt a monomeric conformation, while major ampullate and flagelliform proteins have a preference for dimerization. From an evolutionary perspective, we propose that such dimerization arose to help the processing of disordered silk... (More)

The foundations of silk spinning, the structure, storage, and activation of silk proteins, remain highly debated. By combining solution small-angle neutron and X-ray scattering (SANS and SAXS) alongside circular dichroism (CD), we reveal a shape anisotropy of the four principal native spider silk feedstocks from Nephila edulis. We show that these proteins behave in solution like elongated semiflexible polymers with locally rigid sections. We demonstrated that minor ampullate and cylindriform proteins adopt a monomeric conformation, while major ampullate and flagelliform proteins have a preference for dimerization. From an evolutionary perspective, we propose that such dimerization arose to help the processing of disordered silk proteins. Collectively, our results provide insights into the molecular-scale processing of silk, uncovering a degree of evolutionary convergence in protein structures and chemistry that supports the macroscale micellar/pseudo liquid crystalline spinning mechanisms proposed by the community.

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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomacromolecules
volume
21
issue
8
pages
7 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85089607735
  • pmid:32551521
ISSN
1526-4602
DOI
10.1021/acs.biomac.0c00819
language
English
LU publication?
yes
id
9b57a7d8-aa7c-461a-887e-037c9429f602
date added to LUP
2020-08-27 13:03:52
date last changed
2024-01-17 11:03:31
@article{9b57a7d8-aa7c-461a-887e-037c9429f602,
  abstract     = {{<p>The foundations of silk spinning, the structure, storage, and activation of silk proteins, remain highly debated. By combining solution small-angle neutron and X-ray scattering (SANS and SAXS) alongside circular dichroism (CD), we reveal a shape anisotropy of the four principal native spider silk feedstocks from Nephila edulis. We show that these proteins behave in solution like elongated semiflexible polymers with locally rigid sections. We demonstrated that minor ampullate and cylindriform proteins adopt a monomeric conformation, while major ampullate and flagelliform proteins have a preference for dimerization. From an evolutionary perspective, we propose that such dimerization arose to help the processing of disordered silk proteins. Collectively, our results provide insights into the molecular-scale processing of silk, uncovering a degree of evolutionary convergence in protein structures and chemistry that supports the macroscale micellar/pseudo liquid crystalline spinning mechanisms proposed by the community.</p>}},
  author       = {{Greving, Imke and Terry, Ann E. and Holland, Chris and Boulet-Audet, Maxime and Grillo, Isabelle and Vollrath, Fritz and Dicko, Cedric}},
  issn         = {{1526-4602}},
  language     = {{eng}},
  number       = {{8}},
  pages        = {{3387--3393}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biomacromolecules}},
  title        = {{Structural Diversity of Native Major Ampullate, Minor Ampullate, Cylindriform, and Flagelliform Silk Proteins in Solution}},
  url          = {{http://dx.doi.org/10.1021/acs.biomac.0c00819}},
  doi          = {{10.1021/acs.biomac.0c00819}},
  volume       = {{21}},
  year         = {{2020}},
}