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.

A protein-based bilayer membrane can selectively sequester precious metal ions from leaching solutions of ores and WEEE, and exhibits an adsorption capacity for gold of 1034.4 mg g−1.

No abstract

The ORCID identification number(s) for the author(s) of this article can be found under https://doi.org/10.1002/adma.202104187.A fatal weakness in flexible electronics is the mechanical fracture that occurs during repetitive fatigue deformation; thus, controlling the crack development of the conductive layer is of prime importance and has remained a great challenge until now. Herein, this issue is tackled by utilizing an amyloid/ polysaccharide molecular composite as an interfacial binder. Sodium alginate (SA) can take part in amyloid-like aggregation of the lysozyme, leading to the facile synthesis of a 2D protein/saccharide hybrid nanofilm over an ultralarge area (e.g., >400 cm 2 ). The introduction of SA into amyloid-like aggregates significantly enhances the mechanical strength of the hybrid nanofilm, which, with the help of amyloid-mediated interfacial adhesion, effectively diminishes the microcracks in the hybrid nanofilm coating after repetitive bending or stretching. The microcrack-free hybrid nanofilm then shows high interfacial activity to induce electroless deposition of metal in a Kelvin model on a substrate, which noticeably suppresses the formation of microcracks and consequent conductivity loss during the bending and stretching of the metal-coated flexible substrates. This work underlines the significance of amyloid/polysaccharide nanocomposites in the design of interfacial binders for reliable flexible electronic devices and represents an important contribution to mimicking amyloid and polysaccharide-based adhesive cements created by organisms.

Ap romising route to the synthesis of proteinmimetic materials that are capable of strong mechanics and complex functions is provided by intermolecular b-sheet stacking. An understanding of the assembly mechanism on bsheet stackinga tm olecular-level and the related influencing factors determine the potential to design polymorphs of such biomaterials towards broad applications.Herein, we quantitatively reveal the air/water interface (AWI) parameters regulating the transformation from crowding amorphous aggregates to ordered phase and show that the polymorph diversity of bsheet stacking is regulated by the chain relaxation-crystallization mechanism. An amorphous macroscale amyloid-like nanofilm is formed at the AWI, in which unfolded protein chains are aligned in as hort-range manner to form randomly packed b-sheets.The subsequent biopolymer chain relaxationcrystallization to form nanocrystals is further triggered by removing the limitations of energy and space at the AWI.