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

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

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.

Original languageEnglish (US)
Article number121118
JournalProceedings of the National Academy of Sciences of the United States of America
Volume118
Issue number26
DOIs
StatePublished - Jun 29 2021

All Science Journal Classification (ASJC) codes

  • General

Keywords

  • Electrostatics
  • Landau theory
  • Soft matter
  • Solution assembly
  • Specific ion effects

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