Observation of sequence specificity in the seeding of protein amyloid fibrils
Observation of sequence specificity in the seeding of protein amyloid fibrils
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DOI：
10.1110/ps.04707004
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发表时间：
2004-07-01
期刊：
影响因子：
8
通讯作者：
Dobson, CM
中科院分区：
文献类型：
--
作者：
Krebs, MRH;Morozova-Roche, LA;Dobson, CM
已经确定，淀粉样蛋白形成原纤维的速率通过添加预先形成的原纤维而增强，这种现象称为接种。我们发现，一系列其他蛋白质的鸡溶菌酶的解决方案的种子原纤维形成的效率强烈依赖于它们的序列的相似性。这一观察结果与长程相互作用在稳定淀粉样蛋白原纤维核心结构中的重要性一致，并可能与在传染性海绵状脑病中观察到的种属屏障的存在有关。此外，这与在与每种形式的淀粉样蛋白病相关的沉积物中观察到的单一优势蛋白质类型一致。
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.