Effect of Urea on Biomimetic Systems: Neither Water 3-D Structure Rupture nor Direct Mechanism, Simply a More “Polar Water”

Analysis of a variety of properties of supramolecular aggregates in aqueous urea supports an explanation for the urea effect that differs from traditional explanations based on the direct mechanism of urea−water solvation or the indirect mechanism via rupture of the three-dimensional (3-D) structure of water. The urea-induced effects investigated are increases in amphiphile critical micelle concentrations, ionization degrees (α), and aggregation numbers; decreases in percolation thresholds of reversed micelles; expansion of minimum areas of monolayers; increases in the radii of gyration of polyelectrolytes; changes in morphologies of sodium bis-2-ethylhexylsulfosuccinate thin films on glass substrates; and direct evidence for urea-induced reduction in ion pairing. All of these effects are attributed to an urea-induced enhancement of the hydrophilic properties of water that results in more strongly solvated polar groups and ions and a reduction in ion pair formation. The implications of this analysis for urea effects on protein 3-D structure are briefly highlighted.