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  Collagen pentablock copolymers form smectic liquid crystals as precursors for mussel byssus fabrication

Jehle, F., Priemel, T., Strauss, M., Fratzl, P., Bertinetti, L., & Harrington, M. J. (2021). Collagen pentablock copolymers form smectic liquid crystals as precursors for mussel byssus fabrication. ACS Nano, 15(4), 6829-6838. doi:10.1021/acsnano.0c10457.

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 Creators:
Jehle, Franziska1, Author              
Priemel, Tobias, Author
Strauss, Mike, Author
Fratzl, Peter2, Author              
Bertinetti, Luca3, Author              
Harrington, Matthew J.4, Author              
Affiliations:
1Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863290              
2Peter Fratzl, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863294              
3Luca Bertinetti, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2379691              
4Matthew Harrington, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863292              

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Free keywords: Vesicles, Fibers, Layers, Liquid chromatography, Biopolymers
 Abstract: Protein-based biological materials are important role models for the design and fabrication of next generation advanced polymers. Marine mussels (Mytilus spp.) fabricate hierarchically structured collagenous fibers known as byssal threads via bottom-up supramolecular assembly of fluid protein precursors. The high degree of structural organization in byssal threads is intimately linked to their exceptional toughness and self-healing capacity. Here, we investigated the hypothesis that multidomain collagen precursor proteins, known as preCols, are stored in secretory vesicles as a colloidal liquid crystal (LC) phase prior to thread self-assembly. Using advanced electron microscopy methods, including scanning TEM and FIB-SEM, we visualized the detailed smectic preCol LC nanostructure in 3D, including various LC defects, confirming this hypothesis and providing quantitative insights into the mesophase structure. In light of these findings, we performed an in-depth comparative analysis of preCol protein sequences from multiple Mytilid species revealing that the smectic organization arises from an evolutionarily conserved ABCBA pentablock copolymer-like primary structure based on demarcations in hydropathy and charge distribution as well as terminal pH-responsive domains that trigger fiber formation. These distilled supramolecular assembly principles provide inspiration and strategies for sustainable assembly of nanostructured polymeric materials for potential applications in engineering and biomedical applications.

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Language(s): eng - English
 Dates: 2021-04-012021
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1021/acsnano.0c10457
BibTex Citekey: doi:10.1021/acsnano.0c10457
PMID: 0607
Other: E-Mail OA Info; MS ChemRxiv AP09042021
Other: M:\BM-Publications\2021\JehleACSnano_CollagenPentablock
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Title: ACS Nano
  Other : ACS Nano
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 15 (4) Sequence Number: - Start / End Page: 6829 - 6838 Identifier: ISSN: 1936-0851