Meinhardt J, Fändrich M
Leibniz-Institut für Altersforschung (Fritz-Lipmann-Institut), Jena, Deutschland.
Pathologe. 2009 May;30(3):175-81. doi: 10.1007/s00292-009-1127-2.
Amyloid fibrils are structurally defined as fibrillar polypeptide aggregates with a characteristic cross-beta structure. Such fibrils can be formed by certain polypeptide sequences in the human body and by numerous polypeptide sequences in vitro. All amyloid fibrils possess a structural spine that is formed by a cross-beta structure. This structure is stabilized by hydrogen bonds between the polypeptide backbone. In recent years, various biophysical techniques, such as X-ray crystallography, solid state nuclear magnetic resonance spectroscopy and electron cryo-microscopy have provided insights into the structural organization of amyloid fibrils. This review presents an overview of important results obtained with these methods.
淀粉样纤维在结构上被定义为具有特征性交叉β结构的纤维状多肽聚集体。此类纤维可由人体中的某些多肽序列以及体外的众多多肽序列形成。所有淀粉样纤维都具有由交叉β结构形成的结构骨架。该结构通过多肽主链之间的氢键得以稳定。近年来，各种生物物理技术，如X射线晶体学、固态核磁共振光谱学和电子冷冻显微镜，为淀粉样纤维的结构组织提供了深入见解。本综述概述了通过这些方法获得的重要结果。
