Kazan (Volga Region) Federal University, 18 Kremlevskaya St., 420008, Kazan, Russian Federation.
Magn Reson Chem. 2012 Dec;50(12):784-92. doi: 10.1002/mrc.3880. Epub 2012 Oct 4.
The spatial structure of an active fragment of beta-amyloid Aβ(1-40) heptapeptide Aβ(16-22) (Lys-Leu-Val-Phe-Phe-Ala-Glu) in aqueous buffer solution and in complex with sodium dodecyl sulfate micelles as a model membrane system was investigated by (1)H NMR spectroscopy and two-dimensional NMR (TOCSY, HSQC-HECADE (Heteronuclear Couplings from ASSCI-domain experiments with E.COSY-type crosspeaks), NOESY) spectroscopy. Complex formation was confirmed by the chemical shift changes of the heptapeptide's (1)H NMR spectra, as well as by the signs and values of the NOE effects in different environments. We compared the spatial structure of the heptapeptide in borate buffer solution and in complex with a model of the cell surface membrane.
采用（1）H NMR 光谱和二维 NMR（TOCSY、HSQC-HECADE（具有 ASSCI 域的异核耦合实验与 E.COSY 型交叉峰）、NOESY）光谱研究了在水溶液缓冲液中和与十二烷基硫酸钠胶束作为模型膜系统复合时β-淀粉样蛋白 Aβ（1-40）的活性片段 Aβ（16-22）（Lys-Leu-Val-Phe-Phe-Ala-Glu）的空间结构。通过七肽（1）H NMR 光谱的化学位移变化以及不同环境中 NOE 效应的符号和值，证实了复合物的形成，以及通过七肽（1）H NMR 光谱的化学位移变化以及不同环境中 NOE 效应的符号和值，证实了复合物的形成。我们比较了七肽在硼酸盐缓冲液中和与细胞表面膜模型复合时的空间结构。
