Designer Proteins Self-Assemble into Wires and Lattices on Crystal Surfaces

July 10, 2019

Illustration of epitaxial self-assembly on mica by de novo designed proteins to form a highly ordered hexagonal network. The foreground is based on a computational model of the protein, while the background is derived from an AFM image of protein array with 13.8 nm pores.

Scientific Achievement

De novo designed proteins matched to the crystal structure of mica self-assemble into tunable epitaxial 2D nanostructures.

Significance and Impact

The results demonstrate the ability to systematically program protein-inorganic interfaces to create novel hybrid materials that extend beyond those found in nature.

Research Details

  • Designed an exact match between synthetic protein side chains and the mica surface lattice using Rosetta macromolecular modeling suite.

  • Observed assembly into liquid crystal arrays on mica at single protein resolution using in situ AFM.

  • End-to-end interactions between proteins produced micron-long, single-protein-diameter wires.

  • A trimer interface yielded extensive honeycomb arrays with sides tunable in 3.6 nm increments.

Pyles, H., S. Zhang, J.J. De Yoreo, and D. Baker. (2019). Controlling protein assembly on inorganic crystals through designed protein interfaces. Nature 571: 251-256. DOI: 10.1038/s41586-019-1361-6

Work performed at the University of Washington and Pacific Northwest National Laboratory



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