Ion-dependent protein-surface interactions from intrinsic solvent response.

Autor:	Prelesnik JL; Department of Chemistry, University of Washington, Seattle, WA 98195., Alberstein RG; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093., Zhang S; Physical Sciences Division, Physical and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99354.; Materials Science and Engineering, University of Washington, Seattle, WA 98195., Pyles H; Department of Biochemistry, University of Washington, Seattle, WA 98195.; Institute for Protein Design, University of Washington, Seattle, WA 98195., Baker D; Department of Biochemistry, University of Washington, Seattle, WA 98195.; Institute for Protein Design, University of Washington, Seattle, WA 98195.; HHMI, University of Washington, Seattle, WA 98195., Pfaendtner J; Department of Chemistry, University of Washington, Seattle, WA 98195.; Department of Chemical Engineering, University of Washington, Seattle, WA 98195., De Yoreo JJ; Physical Sciences Division, Physical and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99354.; Materials Science and Engineering, University of Washington, Seattle, WA 98195., Tezcan FA; Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093; chris.mundy@pnnl.gov rick.remsing@rutgers.edu tezcan@ucsd.edu.; Materials Science and Engineering, University of California, San Diego, La Jolla, CA 92093., Remsing RC; Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854; chris.mundy@pnnl.gov rick.remsing@rutgers.edu tezcan@ucsd.edu., Mundy CJ; Department of Chemical Engineering, University of Washington, Seattle, WA 98195; chris.mundy@pnnl.gov rick.remsing@rutgers.edu tezcan@ucsd.edu.; Chemical Physics Theory Team, Pacific Northwest National Laboratory, Richland, WA 99354.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Jun 29; Vol. 118 (26).
DOI:	10.1073/pnas.2025121118
Abstrakt:	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 C98 RhuA). 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. Competing Interests: The authors declare no competing interest.
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu