Amyloid structures at atomic resolution have remained elusive mainly because of their extensive polymorphism and because their polymeric properties have hampered structural studies by classical approaches. Progress in sample preparation, as well as solid-state NMR methods, recently enabled the determination of high-resolution 3D structures of fibrils such as the amyloid-β fibril, which is involved in Alzheimer’s disease. Notably, the simultaneous but independent structure determination of Aβ1-42, a peptide that forms fibrillar deposits in the brain of Alzheimer patients, by two independent laboratories, which yielded virtually identical results, has highlighted how structures can be obtained that allow further functional investigation.

处于原子分辨率的淀粉状蛋白结构仍然难以捉摸，这主要是因为它们具有广泛的多态性，并且由于它们的聚合物性质阻碍了经典方法对结构的研究。样品制备以及固态NMR方法的进展，最近使得能够确定高分辨率的3D结构的原纤维，如淀粉样蛋白β-原纤维，它与阿尔茨海默氏病有关。值得注意的是，由两个独立的实验室同时进行但独立的结构确定Aβ1-42（一种在阿尔茨海默氏病患者脑中形成纤维状沉积物的肽）产生了几乎相同的结果，这突出了如何获得可以进行进一步功能研究的结构。