Details

Autor(en) / Beteiligte

• Miller, Samantha L.
• Levinger, Nancy E.

Titel

Urea Disrupts the AOT Reverse Micelle Structure at Low Temperatures

Ist Teil von

• Langmuir, 2022-06, Vol.38 (24), p.7413-7421

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2022

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Aside from its prominent role in the excretory system, urea is also a known protein denaturant. Here, we characterize urea as it behaves in confined spaces of AOT (sodium bis­(2-ethylhexyl) sulfosuccinate) reverse micelles as a model of tight, confined spaces found at the subcellular level. Dynamic light scattering revealed that low temperatures (275 K) caused the smallest of the reverse micelle sizes, w 0 = 10, to destabilize and dramatically increase in apparent hydrodynamic diameter. We attribute this to urea embedded into the surfactant interface as confirmed by 2D 1H-NOESY NMR spectroscopy. This increase in size in turn caused the hydrogen exchange between urea and water within the nanosized reverse micelles to increase as measured by 1D EXSY-NMR. A minimal enlarging effect and no increase in hydrogen exchange were observed when aqueous urea was introduced into w 0 = 15 or 20 reverse micelles, suggesting that this effect is unique to particularly small-diameter spaces (∼7 nm).