Krebs Mark R H, Morozova-Roche Ludmilla A, Daniel Katie, Robinson Carol V, Dobson Christopher M
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Protein Sci. 2004 Jul;13(7):1933-8. doi: 10.1110/ps.04707004.
It is well established that the rate of formation of fibrils by amyloidogenic proteins is enhanced by the addition of preformed fibrils, a phenomenon known as seeding. We show that the efficiency of seeding fibril formation from solutions of hen lysozyme by a series of other proteins depends strongly on the similarity of their sequences. This observation is consistent with the importance of long-range interactions in stabilizing the core structure of amyloid fibrils and may be associated with the existence of a species barrier observed in the transmissible spongiform encephalopathies. In addition, it is consistent with the observation of a single dominant type of protein in the deposits associated with each form of amyloid disease.
众所周知，通过添加预先形成的纤维，淀粉样蛋白形成纤维的速率会提高，这一现象被称为“种子化”。我们发现，一系列其他蛋白质从溶菌酶溶液中引发纤维形成的效率在很大程度上取决于它们序列的相似性。这一观察结果与长程相互作用在稳定淀粉样纤维核心结构中的重要性相一致，并且可能与在传染性海绵状脑病中观察到的物种屏障的存在有关。此外，这与在每种形式的淀粉样疾病相关沉积物中观察到单一主导类型蛋白质的现象相一致。
