Discrete Orientations of Interfacial Waters Direct Crystallization of Mica-Binding Proteins

Abstract

Understanding the basis of templated molecular assembly on a solid surface requires a fundamental comprehension of both short- and long-range aqueous response to the surface under a variety of solution conditions. Herein we provide a detailed picture of how the molecular-scale response to different mica surfaces yields distinct solvent orientations that produce quasi-static directional potentials onto which macromolecules can adsorb. We connect this directionality to observed (a)symmetric epitaxial alignment of designed proteins onto these surfaces, corroborate our findings with 3D atomic force microscopy experiments, and identify slight differences in surface structure as the origin of this effect. Our work provides a detailed picture of the intrinsic electrolyte response in the vicinity of mineral interfaces, with clear predictions for experiment, and highlights the role of solvent on the predictive assembly of hierarchical materials on mineral surfaces.

Modulating ion-binding at macromolecular interfaces during (bio)mineralization: A snapshot review for calcium carbonate and calcium phosphate systems

“…This group has also extensively studied the folding of macromolecules on mica surfaces [83,84]. For example, Alberstein et al studied the crystallization of proteins on mica and determined that a hydration layer along the surface of the mica likely played a role in templating [85]. Overall, these studies suggest macromolecule-ion binding and hydration can direct crystallization in diverse mineral settings.…”