Fändrich M
Leibniz-Institut für Altersforschung, Beutenbergstrasse 11, 07745, Jena, Germany.
Cell Mol Life Sci. 2007 Aug;64(16):2066-78. doi: 10.1007/s00018-007-7110-2.
Amyloid fibrils occur inside the human body, associated with ageing or a group of diseases that includes, amongst others, Alzheimer's disease, atherosclerosis and type II diabetes. Many natural polypeptide chains are able to form amyloid fibrils in vivo or in vitro, and this ability has been suggested to represent an inherent consequence of the chemical structure of the polypeptide chain. Recent literature has provided a wealth of information about the structure of aggregates, precipitates, amyloid fibrils and other types of fibrillar polypeptide assemblies. However, the biophysical meaning associated with these terms can differ considerably depending on the context of their usage. This overview presents a structural comparison of amyloid fibrils and other types of polypeptide assemblies and defines amyloid fibrils, based on structural considerations, as fibrillar polypeptide aggregates with a cross-beta conformation.
淀粉样纤维出现在人体内部，与衰老或一系列疾病相关，其中包括阿尔茨海默病、动脉粥样硬化和II型糖尿病等。许多天然多肽链能够在体内或体外形成淀粉样纤维，有人认为这种能力是多肽链化学结构的固有结果。最近的文献提供了大量关于聚集体、沉淀物、淀粉样纤维和其他类型的纤维状多肽聚集体结构的信息。然而，与这些术语相关的生物物理意义可能会因使用背景的不同而有很大差异。本综述对淀粉样纤维和其他类型的多肽聚集体进行了结构比较，并基于结构考虑将淀粉样纤维定义为具有交叉β构象的纤维状多肽聚集体。
