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Multiple 2D Materials from a Single Patchy Protein​
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July 28, 2020

Zhang et al Highlight Graphic_Multiple 2

Self-assembly pathways of a patchy protein, L-rhamnulose-1-phosphate aldolase with Cys residues (C98RhuA) into four kinds of 2D lattices held together by disulfide bonds. The AFM images show different crystal morphologies, which are selected by tuning interactions acting over different length scales, formed in solution and on muscovite mica. The crystals formed on mica possess a symmetry element that confers unusual electrical properties that render them piezoelectric.

Scientific Achievement

Used tunable multiscale interactions to assemble a single engineered protein into four distinct 2D crystals and achieve unusual bulk-scale properties.​

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Significance and Impact

Results demonstrate that proteins can be treated as patchy nanoparticles that exhibit rich phase behavior due to a balance of interaction strengths and length scales.

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Research Details

  • For the first time, electric dipole interactions are shown to mediate assembly of proteins in solution.

  • Electrostatic interactions at a charged surface are used to achieve two new 4-fold symmetric crystals.

  • Protein desolvation driven by high potassium concentration leads to a unique bilayer crystal structure.

  • The resulting crystals are electrets that are predicted to exhibit piezoelectric properties.

Zhang, S., R.G. Alberstein, J.J. De Yoreo, and F.A. Tezcan. (2020). Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions. Nature Communications 11: 1-12. DOI: 10.1038/s41467-020-17562-1

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Work performed at Pacific Northwest National Laboratory and the University of California, San Diego

Thrust 1: Emergence of Order: Research

HIGHLIGHT

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