Impact of solvent forces and broken symmetry on the assembly of designed proteins at a liquid-solid interface

Journal Article · Fri Mar 13 00:00:00 EDT 2026 · Nature Communications

DOI:https://doi.org/10.1038/s41467-026-69170-0· OSTI ID:3024106

Yadav Schmid, Sakshi ^[1]; Helfrecht, Benjamin ^[2]; Stegmann, Amy ^[3]; Legg, Benjamin A. ^[2]; Pyles, Harley ^[3]; Chen, Jiajun ^[4]; Edison, John R. ^[5]; Ziatdinov, Maxim ^[6]; Preisler, Zdenek ^[7]; Dollar, Orion ^[8]; Whitelam, Stephen ^[9]; Kalinin, Sergei ^[10]; Baker, David ^[3]; Mundy, Christopher J. ^[11]; Zhang, Shuai ^[11]; De Yoreo, James J. ^[11]

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1. Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Univ. of Washington, Seattle, WA (United States); University of Fribourg (Switzerland); Ecole Polytechnique Federale Lausanne (EPFL) (Switzerland)
2. Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
3. Univ. of Washington, Seattle, WA (United States)
4. Univ. of Washington, Seattle, WA (United States); Mattson Technology, Fremont, CA (United States)
5. Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States); Johns Hopkins Univ., Baltimore, MD (United States)
6. Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Sciences (CNMS)
7. Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States); Inst. of Heritage Science (CNR-ISPC) (Italy)
8. Univ. of Washington, Seattle, WA (United States); Lambic Therapeutics, San Diego, CA (United States)
9. Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
10. Univ. of Tennessee, Knoxville, TN (United States)
11. Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Univ. of Washington, Seattle, WA (United States)

The era of protein design has enabled the creation of hybrid protein-inorganic interfaces, leading to both surface-directed self-assembly of de novo protein architectures and protein-directed formation of inorganic materials. However, the resulting patterns of protein assembly are often unexpected, implying that essential interactions are not accounted for in current design platforms. Here, we use high-speed atomic force microscopy (AFM) analyzed through machine learning to follow the assembly of protein nanorods in aqueous electrolytes on two types of mica exhibiting disparate symmetry elements, which are imprinted on the overlying hydration structure. Using Monte Carlo simulations, we reproduce the observed phases and show that an observed smectic phase, previously thought to be unstable for non-interacting rods in two dimensions, emerges when crystal symmetry introduces a directional bias. The findings demonstrate the importance of incorporating solvent forces as modulated by the hydration structure inherent to interfacial systems when designing protein assemblies at liquid-crystal interfaces. Coupling physics-based simulations that can account for these factors to de novo protein design algorithms can lead to improved design platforms for bio-inspired, hybrid materials.

• Research Organization: Univ. of Washington, Seattle, WA (United States)
• Sponsoring Organization: USDOE Laboratory Directed Research and Development (LDRD) Program; USDOE Office of Science (SC), Basic Energy Sciences (BES)
• Grant/Contract Number: AC02-05CH11231; AC05-76RL01830; SC0018940; SC0019288
• Other Award/Contract Number: FWP 72448
• OSTI ID: 3024106
• Journal Information: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 17; ISSN 2041-1723
• Publisher: Nature Publishing Group
• Country of Publication: United States
• Language: English

Related Subjects

bioinspired materials
nanoscale biophysics