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Self-assembled membrane composed of amyloid-like proteins for efficient size-selective molecular separation and dialysis.


ABSTRACT: The design and scalable construction of robust ultrathin protein membranes with tunable separation properties remain a key challenge in chemistry and materials science. Here, we report a macroscopic ultrathin protein membrane with the potential for scaled-up fabrication and excellent separation efficiency. This membrane, which is formed by fast amyloid-like lysozyme aggregation at air/water interface, has a controllable thickness that can be tuned to 30-250 nm and pores with a mean size that can be tailored from 1.8 to 3.2 nm by the protein concentration. This membrane can retain > 3 nm molecules and particles while permitting the transport of small molecules at a rate that is 1~4 orders of magnitude faster than the rate of existing materials. This membrane further exhibits excellent hemodialysis performance, especially for the removal of middle-molecular-weight uremic toxins, which is 5~6 times higher in the clearance per unit area than the typical literature values reported to date.

SUBMITTER: Yang F 

PROVIDER: S-EPMC6303310 | biostudies-other | 2018 Dec

REPOSITORIES: biostudies-other

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Self-assembled membrane composed of amyloid-like proteins for efficient size-selective molecular separation and dialysis.

Yang Facui F   Tao Fei F   Li Chen C   Gao Lingxiang L   Yang Peng P  

Nature communications 20181221 1


The design and scalable construction of robust ultrathin protein membranes with tunable separation properties remain a key challenge in chemistry and materials science. Here, we report a macroscopic ultrathin protein membrane with the potential for scaled-up fabrication and excellent separation efficiency. This membrane, which is formed by fast amyloid-like lysozyme aggregation at air/water interface, has a controllable thickness that can be tuned to 30-250 nm and pores with a mean size that can  ...[more]

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