首页> 外文期刊>Chembiochem: A European journal of chemical biology >Ordered Langmuir-Blodgett Films of Amphiphilic #beta#-Hairpin Peptides Imaged by Atomic Force Microscopy
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Ordered Langmuir-Blodgett Films of Amphiphilic #beta#-Hairpin Peptides Imaged by Atomic Force Microscopy

机译:原子力显微镜成像的两亲性#beta#-发夹肽的有序Langmuir-Blodgett膜

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摘要

Langmuir and Langmuir-Blodgett (LB) films of peptides have a number of potential applications. The fulfillment of this potential will depend on developing the molecular level undertanding needed to control both the order withing these films and their structures. Self-assembly in thin peptide films can be characterized by circulr dichroism and IR spectroscopies, fluorescence microscopy, and at high resoltion by grazing incidence X-ray diffraction (GIXD), and atomic force microscopy (AFM). Previous fluorescence microscopy results demonstrate that peptide 1 selfassembles into liquid- and solid-phase domains at the air-water (A-W) interface. Here, we have used AFM with carbon nanotube tips to image LB films of 1 and its longer relative, 2. The images show crystalline, two-dimensional order in films of 1 and 2 and demonstrate that the assembly parameters can be varied through well-defined changes in peptide structure.
机译:肽的Langmuir和Langmuir-Blodgett(LB)膜具有许多潜在的应用。这种潜力的实现将取决于开发控制这些膜的顺序及其结构所需的分子水平的弱化。肽薄膜中的自组装可以通过循环二色性和红外光谱,荧光显微镜以及在高分辨下的掠入射X射线衍射(GIXD)和原子力显微镜(AFM)来表征。先前的荧光显微镜结果表明,肽1在空气-水(A-W)界面处自组装成液相和固相域。在这里,我们使用了带有碳纳米管尖端的原子力显微镜,对1和其相对较长的LB薄膜进行了成像。2图像显示了1和2薄膜的结晶二维顺序,并证明了组装参数可以通过适当调整来改变。确定的肽结构变化。

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