The goal of the research, published July 11 in the journal Nature, was to engineer artificial 

proteins to self-assemble on a crystal surface by creating an exact match between the pattern 

of amino acids in the protein and the atoms of the crystal. The ability to program these 

interactions could enable the design of new biomimetic materials with customized colors, 

chemical reactivity or mechanical properties, or to serve as scaffolds for nano-scale filters, 

solar cells or electronic circuits.

"Biology has an amazing ability to organize matter from the atomic scale all the way up to blue 

whales," said co-first author Harley Pyles, a graduate student at the UW Medicine's Institute for 

Protein Design. "Now, using protein design, we can create brand new biomolecules that 

assemble from atomic- to millimeter-length scales. In this case, mica—a naturally occurring 

crystal—is acting like a big Lego baseplate on top of which we are assembling new protein 

architectures."

The design of the new mineral-binding molecules was inspired by proteins that interact with 

ice. At the molecular scale, ice is flat and contains an atomically precise pattern of rigid water 

molecules. In nature, proteins match these patterns to enable them to stick to the ice.

The team used computational molecular design to engineer new proteins with customized 

patterns of electrical charge on their surfaces, as if they were nano-size Lego blocks perfectly 

matched to the mica baseplate. Synthetic genes encoding these designer proteins were placed 

inside bacteria, which then mass produced the proteins in the laboratory.

The researchers found that different designs formed different patterns on the mica surface. By 

redesigning parts of the proteins, the team was able to produce honeycomb lattices in which 

they could digitally tune the diameters of the pores by just a few nanometers, which is about 

the width of a single DNA double helix molecule.