Solvent Isotope Effect on Biomolecular Adsorption at Hydrophobic Surfaces




Jarisz, Tasha A.
Jena, Kailash C.
Dixon, Matthew C.
Hore, Dennis K.

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The Journal of Physical Chemistry C


In vibrational studies of biological systems, D2O is often substituted for H2O to more clearly resolve the amide I and C–H stretching regions. However, in interfacial studies where adsorption is involved, the difference between these two solvents may play a role in the amount adsorbed and, consequently, the adsorbed structure. Nonlinear vibrational spectroscopy reveals striking differences in the spectral signature of the hydrophobic amino acid leucine adsorbed on polystyrene in the presence of light versus heavy water. Dissipation-monitoring quartz crystal microbalance studies conclude that more amino acid is present on the hydrophobic surface when the solvent is D2O, and the relative surface populations account for the difference in spectral intensity. This finding has consequences for surface structural studies, and provides insight into the role of solvent in biomolecular adsorption at hydrophobic surfaces.



Interfaces, Adsorption, Nonlinear optics, Hydrophobicity solvents


Jarisz, T. A.; Jena, K. C.; Dison, M. C.; & Hore, D. K. (2017). Solvent isotope effect on biomolecular adsorption at hydrophobic surfaces. The Journal of Physical Chemistry C, 121(31), 16879-16887. DOI: 10.1021/acs.jpcc.7b05377