Amyloidosis of Alzheimer's Aβ peptides:: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
Amyloidosis of Alzheimer's Aβ peptides:: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
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DOI：
10.1002/mrc.1341
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发表时间：
2004-02-01
影响因子：
2
通讯作者：
Antzutkin, ON
中科院分区：
文献类型：
--
作者：
Antzutkin, ON
讨论了阿尔茨海默病淀粉样蛋白β肽的聚集级联、其与阿尔茨海默病过程中神经毒性的相关性以及对这些研究有用的实验方法。详细的固相肽合成和样品制备程序阿尔茨海默氏症的β-淀粉样蛋白原纤维。从固态NMR和扫描透射电子显微镜（STEM）的数据获得的结构约束的Abeta-原纤维的最新进展进行了讨论。用H-1、C-13固体核磁共振、透射电子显微镜和原子力显微镜研究了Abeta（1-40）“Arctic”突变体的淀粉样原纤维和寡聚体的多态性，并借助原位原子力显微镜观察了不同多晶型肽的实时聚集。最近的结果结合的铜（II）离子和铝-柠檬酸盐和铝-ATP复合物的淀粉样蛋白纤维，研究电子顺磁共振（EPR）和固态Al-27 NMR技术，也提出。版权所有（C）2004约翰威利父子有限公司。
Aggregation cascade for Alzheimer's amyloid-beta peptides, its relevance to neurotoxicity in the course of Alzheimer's disease and experimental methods useful for these studies are discussed. Details of the solid-phase peptide synthesis and sample preparation procedures for Alzheimer's beta-amyloid fibrils are given. Recent progress in obtaining structural constraints on Abeta-fibrils from solid-state NMR and scanning transmission electron microscopy (STEM) data is discussed. Polymorphism of amyloid fibrils and oligomers of the 'Arctic' mutant of Abeta(1-40) was studied by H-1,C-13 solid-state NMR, transmission electron microscopy (TEM) and atomic force microscopy (AFM), and a real-time aggregation of different polymorphs of the peptide was observed with the aid of in situ AFM. Recent results on binding of Cu(II) ions and Al-citrate and Al-ATP complexes to amyloid fibrils, as studied by electron paramagnetic resonance (EPR) and solid-state Al-27 NMR techniques, are also presented. Copyright (C) 2004 John Wiley Sons, Ltd.