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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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Jehle, Franziska1, Autor           
Priemel, Tobias, Autor
Strauss, Mike, Autor
Fratzl, Peter2, Autor           
Bertinetti, Luca3, Autor           
Harrington, Matthew J.4, Autor           
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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Schlagwörter: Vesicles, Fibers, Layers, Liquid chromatography, Biopolymers
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2021-04-012021
 Publikationsstatus: Erschienen
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 Identifikatoren: DOI: 10.1021/acsnano.0c10457
BibTex Citekey: doi:10.1021/acsnano.0c10457
PMID: 0607
Anderer: E-Mail OA Info; MS ChemRxiv AP09042021
Anderer: M:\BM-Publications\2021\JehleACSnano_CollagenPentablock
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Titel: ACS Nano
  Andere : ACS Nano
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, DC : American Chemical Society
Seiten: - Band / Heft: 15 (4) Artikelnummer: - Start- / Endseite: 6829 - 6838 Identifikator: ISSN: 1936-0851