| Title: |
Ion-dependent protein–surface interactions from intrinsic solvent response |
| Authors: |
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 |
| Source: |
Proceedings of the National Academy of Sciences of the United States of America, vol 118, iss 26 |
| Publisher Information: |
eScholarship, University of California |
| Publication Year: |
2021 |
| Collection: |
University of California: eScholarship |
| Subject Terms: |
3403 Macromolecular and Materials Chemistry (for-2020); 34 Chemical Sciences (for-2020); 3406 Physical Chemistry (for-2020); Bioengineering (rcdc); Aluminum Silicates (mesh); Ions (mesh); Microscopy; Atomic Force (mesh); Probability (mesh); Proteins (mesh); Solvents (mesh); Surface Properties (mesh); Water (mesh); soft matter; solution assembly; specific ion effects; electrostatics; Landau theory |
| Description: |
The phyllosilicate mineral muscovite mica is widely used as a surface template for the patterning of macromolecules, yet a molecular understanding of its surface chemistry under varying solution conditions, required to predict and control the self-assembly of adsorbed species, is lacking. We utilize all-atom molecular dynamics simulations in conjunction with an electrostatic analysis based in local molecular field theory that affords a clean separation of long-range and short-range electrostatics. Using water polarization response as a measure of the electric fields that arise from patterned, surface-bound ions that direct the adsorption of charged macromolecules, we apply a Landau theory of forces induced by asymmetrically polarized surfaces to compute protein-surface interactions for two muscovite-binding proteins (DHR10-mica6 and C98RhuA). Comparison of the pressure between surface and protein in high-concentration KCl and NaCl aqueous solutions reveals ion-specific differences in far-field protein-surface interactions, neatly capturing the ability of ions to modulate the surface charge of muscovite that in turn selectively attracts one binding face of each protein over all others. |
| Document Type: |
article in journal/newspaper |
| File Description: |
application/pdf |
| Language: |
unknown |
| Relation: |
qt835792gz; https://escholarship.org/uc/item/835792gz; https://escholarship.org/content/qt835792gz/qt835792gz.pdf |
| DOI: |
10.1073/pnas.2025121118 |
| Availability: |
https://escholarship.org/uc/item/835792gz; https://escholarship.org/content/qt835792gz/qt835792gz.pdf; https://doi.org/10.1073/pnas.2025121118 |
| Rights: |
public |
| Accession Number: |
edsbas.9A4380FB |
| Database: |
BASE |