Krysmann M J, Castelletto V, McKendrick J E, Clifton L A, W Hamley I, Harris P J F, King S M
Department of Chemistry, University of Reading, Reading, UK.
Langmuir. 2008 Aug 5;24(15):8158-62. doi: 10.1021/la800942n. Epub 2008 Jun 21.
The self-assembly of a modified fragment of the amyloid beta peptide, based on sequence Abeta(16-20), KLVFF, extended to give AAKLVFF is studied in methanol. Self-assembly into peptide nanotubes is observed, as confirmed by electron microscopy and small-angle X-ray scattering. The secondary structure of the peptide is probed by FTIR and circular dichroism, and UV/visible spectroscopy provides evidence for the important role of aromatic interactions between phenylalanine residues in driving beta-sheet self-assembly. The beta-sheets wrap helically to form the nanotubes, the nanotube wall comprising four wrapped beta-sheets. At higher concentration, the peptide nanotubes form a nematic phase that exhibits spontaneous flow alignment as observed by small-angle neutron scattering.
基于序列Abeta(16 - 20)、KLVFF并扩展为AAKLVFF的β-淀粉样肽修饰片段在甲醇中的自组装过程得到了研究。通过电子显微镜和小角X射线散射证实，该片段自组装形成了肽纳米管。利用傅里叶变换红外光谱（FTIR）和圆二色性对肽的二级结构进行了探测，紫外/可见光谱则为苯丙氨酸残基之间的芳香族相互作用在驱动β-折叠自组装过程中的重要作用提供了证据。β-折叠呈螺旋状包裹形成纳米管，纳米管壁由四个包裹的β-折叠组成。在较高浓度下，肽纳米管形成向列相，小角中子散射观察到其呈现出自发的流动取向。
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