Impact of solvent forces and broken symmetry on the assembly of designed proteins at a liquid-solid interface
Year: 2026
Type: article
Abstract: 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.
Source: Nature Communications
Institutions: Pacific Northwest National Laboratory, University of Fribourg, University of Washington, École Polytechnique Fédérale de Lausanne, Johns Hopkins University, Lawrence Berkeley National Laboratory, Molecular Foundry, Oak Ridge National Laboratory, Center for Nanophase Materials Sciences, National Research Council, University of Tennessee at Knoxville, Howard Hughes Medical Institute
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $6,990
Funders: National Science Foundation, U.S. Department of Energy, Battelle, Indian Institute of Science, University of Washington, Indian National Science Academy, Indian Institute of Science Education and Research Mohali, Office of Science, Basic Energy Sciences, Oak Ridge National Laboratory, Lawrence Berkeley National Laboratory, Pacific Northwest National Laboratory
Awards: G1079818582, G1143651532, G125460123, G1286236842, G1286251239, G138090931, G1851334662, G1863003419, G1899721271, G2506945562, G2510423872, G2618837358, G2988778103, G30714459, G3083819904, G3107502785, G3349933317, G3481556109, G391136020, CSSAS: THE CENTER FOR THE SCIENCE OF SYNTHESIS ACROSS SCALES, G419881185, G42916606, G4501827968, Graduate Research Fellowship Program (GRFP), G498139845, G5321382714, G5558627913, G5653134238, G5726405315, G613759197, G650090426, G653274256, G660579501, G6652958823, G7148496000, PRINCIPLES OF DE NOVO PROTEIN NANOMATERIAL ASSEMBLY IN 1, 2 AND 3 DIMENSIONS, G7354628648, G7560550554, G7665161096, G8135867528, G821644656, G8287742688, G8446353467, Graduate Research Fellowship Program (GRFP), G969889393
OpenAlex ID: W7135194059