Xu Shaohua
Biological Sciences Department, Florida Institute of Technology, Melbourne, FL 32901, USA.
Amyloid. 2007 Jun;14(2):119-31. doi: 10.1080/13506120701260059.
Protein amyloid fibers are often found to have a beta-pleated sheet structure regardless of their sequence, leading some to believe that it is the molecule's misfolding that leads to aggregation. In this article, an alternative model is introduced for the amyloid community to consider, that fiber formation is a surface-energy minimization process, starting with the generation of colloidal particles and their linear assembly, and ending with structural evolution of the aggregates into mature fibers. We propose that aggregation drives conformational change and that a conformational change is not essential to initiate the aggregation process.
蛋白质淀粉样纤维无论其序列如何，通常都具有β折叠片层结构，这使得一些人认为是分子的错误折叠导致了聚集。在本文中，为淀粉样蛋白领域引入了另一种模型供其考虑，即纤维形成是一个表面能最小化过程，始于胶体颗粒的产生及其线性组装，终于聚集体向成熟纤维的结构演化。我们提出聚集驱动构象变化，并且构象变化对于启动聚集过程并非必不可少。
