Kazan Federal University, 18 Kremlevskaya St., Kazan, 420008, Russian Federation,
Eur Biophys J. 2013 Dec;42(11-12):803-10. doi: 10.1007/s00249-013-0928-7. Epub 2013 Sep 15.
The spatial structure of Alzheimer's amyloid Aβ10-35-NH2 peptide in aqueous solution at pH 7.3 and in SDS micelles was investigated by use of a combination of the residual dipolar coupling method and two-dimensional NMR spectroscopy (TOCSY, NOESY). At pH 7.3 Aβ10-35-NH2 adopts a compact random-coil conformation whereas in SDS micellar solutions two helical regions (residues 13-23 and 30-35) of Aβ10-35-NH2 were observed. By use of experimental data, the structure of "peptide-micelle" complex was determined; it was found that Aβ10-35-NH2 peptide binds to the micelle surface at two regions (residues 17-20 and 29-35).
在 pH 7.3 时水溶液中和在 SDS 胶束中，通过使用残剩偶极耦合方法和二维 NMR 光谱（TOCSY、NOESY）联合的方法，研究了阿尔茨海默氏症淀粉样蛋白 Aβ10-35-NH2 在水中的空间结构。在 pH 7.3 时，Aβ10-35-NH2 采取紧凑的无规卷曲构象，而在 SDS 胶束溶液中观察到 Aβ10-35-NH2 的两个螺旋区域（残基 13-23 和 30-35）。利用实验数据，确定了“肽-胶束”复合物的结构；发现 Aβ10-35-NH2 肽在两个区域（残基 17-20 和 29-35）结合到胶束表面。
