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Publications of the Week

Controlling Protein Assembly on Inorganic Crystals through Designed Protein Interfaces

By July 22, 2019No Comments

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This week we profile a recent publication in Nature from Harley Pyles (pictured)
in the laboratory of Dr. David Baker at the Institute for Protein Design at UW.

Can you provide a brief overview of your lab’s current research focus?

The Baker lab is focused on the design of protein from scratch. We use both computation design tools and experimental testing to create new molecules for a wide range of applications, including cancer immunotherapy, infectious disease prevention, basic research and more.

What is the significance of the findings in this publication?

Many hard biomaterials like bone and teeth get their exquisite material properties from protein–mineral interactions. In this paper, we show that new, precise protein–mineral interactions can be programmed from first principles. Together with collaborators at the Pacific Northwest National Laboratory, we were able to create rod- and honeycomb-like arrays that self-assemble on the atomic surface of mica, a common and exceptionally smooth mineral.

Graduate student and lead author Harley Pyles says:“Biology has an amazing ability to organize matter from the atomic scale all the way up to blue whales. 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.”

What are the next steps for this research?

This is only the beginning of designed protein hybrid materials. Taken together with other recent developments in the design of 1D and 2D protein assemblies, we believe we’re on the verge of seeing many new classes of highly customizable biomaterials. These could have applications in medicine, manufacturing and more.

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