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  Phase transitions as intermediate steps in the formation of molecularly engineered protein fibers

Mohammadi, P., Aranko, A. S., Lemetti, L., Cenev, Z., Zhou, Q., Virtanen, S., et al. (2018). Phase transitions as intermediate steps in the formation of molecularly engineered protein fibers. Communications Biology, 1(1): 86. doi:10.1038/s42003-018-0090-y.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-AA81-D Version Permalink: http://hdl.handle.net/21.11116/0000-0001-AA82-C
Genre: Journal Article

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 Creators:
Mohammadi, Pezhman, Author
Aranko, A. Sesilja, Author
Lemetti, Laura, Author
Cenev, Zoran, Author
Zhou, Quan, Author
Virtanen, Salla, Author
Landowski, Christopher P., Author
Penttilä, Merja, Author
Fischer, Wolfgang J., Author
Wagermaier, Wolfgang1, Author              
Linder, Markus B., Author
Affiliations:
1Wolfgang Wagermaier, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863296              

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 Abstract: A central concept in molecular bioscience is how structure formation at different length scales is achieved. Here we use spider silk protein as a model to design new recombinant proteins that assemble into fibers. We made proteins with a three-block architecture with folded globular domains at each terminus of a truncated repetitive silk sequence. Aqueous solutions of these engineered proteins undergo liquid–liquid phase separation as an essential pre-assembly step before fibers can form by drawing in air. We show that two different forms of phase separation occur depending on solution conditions, but only one form leads to fiber assembly. Structural variants with one-block or two-block architectures do not lead to fibers. Fibers show strong adhesion to surfaces and self-fusing properties when placed into contact with each other. Our results show a link between protein architecture and phase separation behavior suggesting a general approach for understanding protein assembly from dilute solutions into functional structures.

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 Dates: 2018-07-02
 Publication Status: Published in print
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 Identifiers: DOI: 10.1038/s42003-018-0090-y
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Title: Communications Biology
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 1 (1) Sequence Number: 86 Start / End Page: - Identifier: ISSN: 2399-3642