Hydrophobic interactions are considered to play a key role in biological processes ranging from membrane formation to protein folding and ligand binding, and yet little is known regarding water's role in mediating such interactions. In order to directly probe hydration-shell water structural changes upon hydrophobic aggregation, we have combining Raman spectroscopy and multivariate curve resolution (Raman-MCR). Hydration-shell spectra obtained from aqueous alcohol and surfactant solutions reveal water structure changes induced by alcohol aggregation and micelle formation. More specifically, we are able to track the appearance of both water-separated aggregates and direct-hydrophobic contact aggregates with increasing solute concentration. Our findings indicate that hydrophobic groups do not shed their hydration-shells as readily as one might have expected.

Hydration-shell spectroscopic studies of water mediated hydrophobic interactions

246th National Meeting (2013)

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