Litcius/Paper detail

Ion-dependent protein–surface interactions from intrinsic solvent response

Jesse L. Prelesnik, Robert G. Alberstein, Shuai Zhang, Harley Pyles, David Baker, Jim Pfaendtner, James J. De Yoreo, F. Akif Tezcan, Richard C. Remsing, Christopher J. Mundy

2021Proceedings of the National Academy of Sciences21 citationsDOIOpen Access PDF

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.

Topics & Concepts

MuscoviteChemical physicsElectrostaticsMolecular dynamicsMacromoleculeIonAdsorptionMicaChemistryStatic electricitySurface chargeAqueous solutionProtein adsorptionSurface forces apparatusComputational chemistryMaterials sciencePhysical chemistryOrganic chemistryPhysicsComposite materialBiochemistryQuartzQuantum mechanicsForce Microscopy Techniques and ApplicationsElectrostatics and Colloid InteractionsSpectroscopy and Quantum Chemical Studies