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Exploiting mammalian low-complexity domains for liquid-liquid phase separation-driven underwater adhesive coatings.


ABSTRACT: Many biological materials form via liquid-liquid phase separation (LLPS), followed by maturation into a solid-like state. Here, using a biologically inspired assembly mechanism designed to recapitulate these sequential assemblies, we develop ultrastrong underwater adhesives made from engineered proteins containing mammalian low-complexity (LC) domains. We show that LC domain-mediated LLPS and maturation substantially promotes the wetting, adsorption, priming, and formation of dense, uniform amyloid nanofiber coatings on diverse surfaces (e.g., Teflon), and even penetrating difficult-to-access locations such as the interiors of microfluidic devices. Notably, these coatings can be deposited on substrates over a broad range of pH values (3 to 11) and salt concentrations (up to 1 M NaCl) and exhibit strong underwater adhesion performance. Beyond demonstrating the utility of mammalian LC domains for driving LLPS in soft materials applications, our study illustrates a powerful example of how combining LLPS with subsequent maturation steps can be harnessed for engineering protein-based materials.

SUBMITTER: Cui M 

PROVIDER: S-EPMC6707783 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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Exploiting mammalian low-complexity domains for liquid-liquid phase separation-driven underwater adhesive coatings.

Cui Mengkui M   Wang Xinyu X   An Bolin B   Zhang Chen C   Gui Xinrui X   Li Ke K   Li Yingfeng Y   Ge Peng P   Zhang Junhu J   Liu Cong C   Zhong Chao C  

Science advances 20190823 8


Many biological materials form via liquid-liquid phase separation (LLPS), followed by maturation into a solid-like state. Here, using a biologically inspired assembly mechanism designed to recapitulate these sequential assemblies, we develop ultrastrong underwater adhesives made from engineered proteins containing mammalian low-complexity (LC) domains. We show that LC domain-mediated LLPS and maturation substantially promotes the wetting, adsorption, priming, and formation of dense, uniform amyl  ...[more]

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