The discovery of a general strategy for organizing functional proteins into stable nanostructures with the desired dimension, shape, and function is an important focus in developing protein-based self-assembled materials, but the scalable synthesis of such materials and transfer to other substrates remain great challenges. We herein tackle this issue by creating a two-dimensional metal–protein hybrid nanofilm that is flexible and cost-effective with reliable self-recovery, stability, and multifunctionality. As it differs from traditional metal ions, we discover the capability of Sn2+ to initiate fast amyloid-like protein assembly (occurring in seconds) by effectively reducing the disulfide bonds of native globular proteins. The Sn2+-initiated lysozyme aggregation at the air/water interface leads to droplet flattening, a result never before reported in a protein system, which finally affords a multifunctional 2D Sn-doped hybrid lysozyme nanofilm with an ultralarge area (e.g., 0.2 m2) within a few minutes. The hybrid film is distinctive in its ease of coating on versatile material surfaces with endurable chemical and mechanical stability, optical transparency, and diverse end uses in antimicrobial and photo-/electrocatalytic scaffolds. Our approach provides not only insights into the effect of tin ions on macroscopic self-assembly of proteins but also a controllable and scalable synthesis of a potential biomimic framework for biomedical and biocatalytic applications.
ACS Nano, Sn-Triggered Two-Dimensional Fast Protein Assembly with Emergent Functions, 2019, ASAP