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Nonlinear scaling of surface water diffusion with bulk water viscosity of crowded solutions.

ABSTRACT: The translational hydration dynamics within 0.5-1.5 nm of the surface of a DPPC liposome, a model biomacromolecular surface, is analyzed by the recently developed Overhauser dynamic nuclear polarization (ODNP) technique. We find that dramatic changes to the bulk solvent cause only weak changes in the surface hydration dynamics. Specifically, both a >10-fold increase in bulk viscosity and the restriction of diffusion by confinement on a multiple nm length-scale change the local translational diffusion coefficient of the surface water surrounding the lipid bilayer by <2.5-fold. By contrast, previous ODNP studies have shown that changes to the biomacromolecular surface induced by folding, binding, or aggregation can cause local hydration dynamics to vary by factors of up to 30. We suggest that the surface topology and chemistry at the ?1.5 nm scale, rather than the characteristics of the solvent, nearly exclusively determine the macromolecule's surface hydration dynamics.

SUBMITTER: Franck JM

PROVIDER: S-EPMC3785640 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Nonlinear scaling of surface water diffusion with bulk water viscosity of crowded solutions.

Franck John M JM Scott John A JA Han Songi S

Journal of the American Chemical Society 20130311 11

The translational hydration dynamics within 0.5-1.5 nm of the surface of a DPPC liposome, a model biomacromolecular surface, is analyzed by the recently developed Overhauser dynamic nuclear polarization (ODNP) technique. We find that dramatic changes to the bulk solvent cause only weak changes in the surface hydration dynamics. Specifically, both a >10-fold increase in bulk viscosity and the restriction of diffusion by confinement on a multiple nm length-scale change the local translational diff ...[more]

PMID: 23347324

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