Urea Disrupts the AOT Reverse Micelle Structure at Low Temperatures
Urea Disrupts the AOT Reverse Micelle Structure at Low Temperatures
复制标题
尿素在低温下破坏 AOT 反胶束结构
DOI:
10.1021/acs.langmuir.2c00206
复制
发表时间:
2022
期刊:
影响因子:
3.9
通讯作者:
Levinger, Nancy E.
中科院分区:
文献类型:
--
作者:
Miller, Samantha L.;Levinger, Nancy E.
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,w0= 10, to destabilize and dramatically increase in apparent hydrodynamic diameter. We attribute this to urea embedded into the surfactant interface as confirmed by 2D1H-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 intow0= 15 or 20 reverse micelles, suggesting that this effect is unique to particularly small-diameter spaces (∼7 nm).