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


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
29 06 2021
Historique:
entrez: 26 6 2021
pubmed: 27 6 2021
medline: 15 12 2021
Statut: ppublish

Résumé

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

Identifiants

pubmed: 34172582
pii: 2025121118
doi: 10.1073/pnas.2025121118
pmc: PMC8255788
pii:
doi:

Substances chimiques

Aluminum Silicates 0
Ions 0
Proteins 0
Solvents 0
muscovite 0
Water 059QF0KO0R
mica V8A1AW0880

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Jesse L Prelesnik (JL)

Department of Chemistry, University of Washington, Seattle, WA 98195.

Robert G Alberstein (RG)

Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093.

Shuai 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.

Harley Pyles (H)

Department of Biochemistry, University of Washington, Seattle, WA 98195.
Institute for Protein Design, University of Washington, Seattle, WA 98195.

David 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.

Jim Pfaendtner (J)

Department of Chemistry, University of Washington, Seattle, WA 98195.
Department of Chemical Engineering, University of Washington, Seattle, WA 98195.

James J 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.

F Akif 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.

Richard C Remsing (RC)

Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854; chris.mundy@pnnl.gov rick.remsing@rutgers.edu tezcan@ucsd.edu.

Christopher J 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.

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