Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
J Am Soc Mass Spectrom. 2010 Jul;21(7):1087-96. doi: 10.1016/j.jasms.2010.02.026. Epub 2010 Mar 9.
A number of proteins are capable of converting from their soluble, monomeric form into highly-ordered, insoluble aggregates known as amyloid fibrils. In vivo, these fibrils, which accumulate in organs and tissues, are associated with a wide range of amyloid diseases for which there are currently no therapeutic solutions. The molecular details of the pathway from native monomer through oligomeric intermediates to the final amyloid fibril remain a challenging enigma. Over the past few years, mass spectrometry has been applied to investigate the various stages of amyloid fibril formation, and this report summarizes the key steps achieved to date.
许多蛋白质能够从可溶性单体形式转化为高度有序的不溶性聚集物，称为淀粉样纤维。在体内，这些纤维在器官和组织中积累，与广泛的淀粉样疾病有关，目前尚无治疗方法。从天然单体通过寡聚中间体到最终淀粉样纤维的途径的分子细节仍然是一个具有挑战性的谜。在过去的几年中，质谱已被应用于研究淀粉样纤维形成的各个阶段，本报告总结了迄今为止取得的关键步骤。
