DOE OSTI · 1798553
Ion-dependent protein–surface interactions from intrinsic solvent response
Abstract
Significance Hard–soft interfaces between inorganic surfaces and biomolecules promote self-assembly processes with broad implications in biogeochemistry, energy sciences, nanomedicine, and origins of life. Yet, detailed molecular-scale understanding of inorganic–biomolecule interactions and their dependence on solution conditions is missing. We present a theory for the initial stages of inorganic–biomolecule assembly based on the far-field response of water, using experimentally characterized interactions between muscovite surfaces and mica-binding proteins as model systems. Our work connects molecular details of the solution to assembly outcomes and suggests the initial driving forces for assembly are dominated by long-range, ion-specific interactions. The connections made between interfacial structure and long-range surface–biomolecule interactions provide insights toward a predictive understanding of biomolecular self-assembly on mineral surfaces.
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Prelesnik, Jesse L., Alberstein, Robert G., Zhang, Shuai, Pyles, Harley, Baker, David, Pfaendtner, Jim, De Yoreo, James J., Tezcan, F. Akif, Remsing, Richard C., Mundy, Christopher J.. 2021-06-25. Ion-dependent protein–surface interactions from intrinsic solvent response. https://doi.org/10.1073/pnas.2025121118
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