Two-dimensional materials, the first Nature article of the year

First author by Ariel J. Ben-Sasson

Corresponding authors: David Baker and Emmanuel Derivery

Communication unit: University of Washington, MRC Molecular Biology Laboratory, Cambridge

Research Highlights:

1. A new method for computational control of binary protein two-dimensional material assembly was developed.

2. Realize the construction of ordered two-dimensional arrays on disordered substrates.

Two-dimensional materials, promising potential. Even biologists have become interested in two-dimensional materials.

Ordered two-dimensional protein materials form a single lattice from flexible links, which tend to consist of only one protein component. Naturally, scientists felt that a material consisting of two protein components was more advantageous.

Hereditary programmable materials that spontaneously coassemble into ordered structures after mixing two or more components are easier to control than materials composed of two or more components. It is easier for scientists to regulate assembly dynamics, rigorously characterize and manipulate parts, and implement more complex functions, allowing the system to be used in a variety of applications.

Two-dimensional ordered arrays of binary components have been confirmed, but due to the flexibility of the components, the structure of the design material cannot be fully determined in advance, and the building elements have dihedral symmetry, and the arrays have the same upper and lower surfaces. De novo design between rigid domains stabilized through extensive non-covalent interactions will provide more control over atomic structure and provide a reliable starting point for further structural and functional adjustments.

In view of this, David Baker of the University of Washington and Emmanuel Derivery of the MRC Laboratory of Molecular Biology in Cambridge et al. report a computational method that can generate co-assembled binary layers to achieve binary protein two-dimensional superlattices by designing rigid interfaces between paired dihedral protein building units.