Molecular rearrangement of metal-chelating lipid monolayers upon protein adsorption.
Molecular rearrangement of metal-chelating lipid monolayers upon protein adsorption.
复制标题
蛋白质吸附后金属螯合脂质单层的分子重排。
DOI：
10.1021/la902052f
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发表时间：
2010
期刊：
影响因子：
--
通讯作者：
Rabolt,JohnF
中科院分区：
文献类型：
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作者：
Kim,YoungShin;Chase,Bruce;Kiick,KristiL;Rabolt,JohnF
控制蛋白质吸附到明确的单分子膜是至关重要的传感器和纳米技术应用的进展，其中目标物种的选择性吸附是感兴趣的。在这里报道的研究中，我们开发了振动光谱方法，以获得对蛋白质与空气-水界面处的金属螯合单层的单位点与多位点结合的影响的分子洞察。实时平面阵列红外反射-吸收光谱分析显示，Cu（II）螯合DSIDA脂质单层（Cu 2 +-DSIDA）很容易被肌红蛋白吸附破坏，如thevas（CH 2）拉伸模式蓝移1.7 cm− 1和5 h内峰强度降低所示。然而，锌（II）螯合单层不受任何蛋白质的吸附，这表明多位点结合的蛋白质上的Cu 2 +-DSIDA的结果在单层破坏。进一步的研究表明，肌红蛋白在膜上的吸附对肌红蛋白的二级结构，尤其是α-螺旋结构、无规结构和伸展结构产生了扰动。而在吸附溶菌酶的过程中，没有观察到明显的变化。这些结果表明，这些方法用于监测金属带电的脂质单层和蛋白质的分子重排，发生在吸附的蛋白质具有很强的亲和力的单层的效用。
The controlled adsorption of proteins to well-defined monolayers is critical to advances in sensor and nanotechnology applications where selective adsorption of targeted species is of interest. In the studies reported here, we developed vibrational spectroscopic methods to gain molecular insight into the effect of single-site versus multiple-site binding of proteins to metal-chelating monolayers at an air−water interface. Analysis of real-time planar array infrared reflection−absorption spectra revealed that a Cu(II)-chelated DSIDA lipid monolayer (Cu2+-DSIDA) was readily disrupted by adsorption of myoglobin as demonstrated by a blue shift of 1.7 cm−1in thevas(CH2) stretching mode and a reduced peak intensity over a period of 5 h. However, a Zn(II)-chelated monolayer was not affected by the adsorption of either protein, suggesting that multisite binding of protein on the Cu2+-DSIDA results in monolayer disruption. Further studies demonstrated that in film form, adsorption of myoglobin to the Cu2+-DSIDA perturbed the secondary structures of myoglobin, especially the α-helical, random structure, and extended structures. However, no distinct change was observed during adsorption of lysozyme. These results demonstrate the utility of these methods for monitoring the molecular rearrangement of both metal-charged lipid monolayers and proteins that occur during adsorption of a protein with a strong affinity for the monolayer.