Department of Pharmacology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, USA.
J Biol Chem. 2011 May 13;286(19):16533-40. doi: 10.1074/jbc.R111.227108. Epub 2011 Mar 25.
Amyloid is traditionally viewed as a consequence of protein misfolding and aggregation and is most notorious for its association with debilitating and chronic human diseases. However, a growing list of examples of "functional amyloid" challenges this bad reputation and indicates that many organisms can employ the biophysical properties of amyloid for their benefit. Because of developments in the structural studies of amyloid, a clearer picture is emerging about what defines amyloid structure and the properties that unite functional and pathological amyloids. Here, we review various amyloids and place them within the framework of the latest structural models.
淀粉样蛋白传统上被视为蛋白质错误折叠和聚集的结果,因其与使人衰弱和慢性的人类疾病有关而声名狼藉。然而,越来越多的“功能性淀粉样蛋白”的例子挑战了这种恶名,并表明许多生物体可以利用淀粉样蛋白的物理特性从中受益。由于淀粉样蛋白结构研究的发展,对于定义淀粉样蛋白结构以及将功能性和病理性淀粉样蛋白联系起来的特性,我们有了更清晰的认识。在这里,我们综述了各种淀粉样蛋白,并将它们置于最新结构模型的框架内。