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

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.

Authors:
ORCiD logo; ORCiD logo; ORCiD logo; ORCiD logo
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States); Univ. of Washington, Seattle, WA (United States); Univ. of California, San Diego, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Materials Sciences & Engineering Division; National Science Foundation (NSF)
OSTI Identifier:
1643727
Alternate Identifier(s):
OSTI ID: 1650710; OSTI ID: 1668312; OSTI ID: 1781109
Report Number(s):
PNNL-SA-153945
Journal ID: ISSN 2041-1723; 3770; PII: 17562
Grant/Contract Number:  
SC0019288; SC0003844; AC05-76RL01830
Resource Type:
Published Article
Journal Name:
Nature Communications
Additional Journal Information:
Journal Name: Nature Communications Journal Volume: 11 Journal Issue: 1; Journal ID: ISSN 2041-1723
Publisher:
Nature Publishing Group
Country of Publication:
United Kingdom
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; atomic force microscopy; biomaterials; biophysics; nanoscale materials; surface assembly

Citation Formats

Zhang, Shuai, Alberstein, Robert G., De Yoreo, James J., and Tezcan, F. Akif. Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions. United Kingdom: N. p., 2020. Web. doi:10.1038/s41467-020-17562-1.
Zhang, Shuai, Alberstein, Robert G., De Yoreo, James J., & Tezcan, F. Akif. Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions. United Kingdom. https://doi.org/10.1038/s41467-020-17562-1
Zhang, Shuai, Alberstein, Robert G., De Yoreo, James J., and Tezcan, F. Akif. Tue . "Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions". United Kingdom. https://doi.org/10.1038/s41467-020-17562-1.
@article{osti_1643727,
title = {Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions},
author = {Zhang, Shuai and Alberstein, Robert G. and De Yoreo, James J. and Tezcan, F. Akif},
abstractNote = {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.},
doi = {10.1038/s41467-020-17562-1},
journal = {Nature Communications},
number = 1,
volume = 11,
place = {United Kingdom},
year = {Tue Jul 28 00:00:00 EDT 2020},
month = {Tue Jul 28 00:00:00 EDT 2020}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1038/s41467-020-17562-1

Citation Metrics:
Cited by: 19 works
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