Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions

Shuai Zhang, Robert G. Alberstein, James J. Yoreo () and F. Akif Tezcan ()
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Shuai Zhang: University of Washington
Robert G. Alberstein: University of California, San Diego
James J. Yoreo: University of Washington
F. Akif Tezcan: University of California, San Diego

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract Self-assembly of molecular building blocks into higher-order structures is exploited in living systems to create functional complexity and represents a powerful strategy for constructing new materials. As nanoscale building blocks, proteins offer unique advantages, including monodispersity and atomically tunable interactions. Yet, control of protein self-assembly has been limited compared to inorganic or polymeric nanoparticles, which lack such attributes. Here, we report modular self-assembly of an engineered protein into four physicochemically distinct, precisely patterned 2D crystals via control of four classes of interactions spanning Ångström to several-nanometer length scales. We relate the resulting structures to the underlying free-energy landscape by combining in-situ atomic force microscopy observations of assembly with thermodynamic analyses of protein-protein and -surface interactions. Our results demonstrate rich phase behavior obtainable from a single, highly patchy protein when interactions acting over multiple length scales are exploited and predict unusual bulk-scale properties for protein-based materials that ensue from such control.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17562-1

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DOI: 10.1038/s41467-020-17562-1

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