Taboada Pablo, Barbosa Silvia, Castro Emilio, Mosquera Víctor
J Phys Chem B. 2006 Oct 26;110(42):20733-6. doi: 10.1021/jp064861r.
Under in vitro solution conditions where the native state is destabilized, many proteins present an abnormal structure and metabolism associated with a strong tendency to self-aggregation into a polymeric amyloid fibril structure, suggesting that this ability is a generic feature of the polypeptide chains. Such structures play a key role in different pathogenesis of neurodegenerative diseases such as Alzheimer, Parkinson, or Creutzfeldt-Jakob. Here, we report the formation of amyloid fibrils in the plasma protein human serum albumin under different in vitro conditions monitored using a combination of spectrophotometric and microscopic techniques. Amyloid fibril formation, therefore, is also allowed in a protein with a high degree of structural complexity. We also infer from experimental data the existence of other protein aggregated species than fibrils, some of which seem to be formed by a structural rearrangement of the proper fibrils.
在天然状态不稳定的体外溶液条件下，许多蛋白质呈现出异常的结构和代谢，具有强烈的自我聚集形成聚合物淀粉样纤维结构的倾向，这表明这种能力是多肽链的一个普遍特征。此类结构在阿尔茨海默病、帕金森病或克雅氏病等不同神经退行性疾病的发病机制中起关键作用。在此，我们报告了在不同体外条件下，使用分光光度法和显微镜技术相结合监测到的血浆蛋白人血清白蛋白中淀粉样纤维的形成。因此，在具有高度结构复杂性的蛋白质中也会形成淀粉样纤维。我们还从实验数据推断出除纤维之外还存在其他蛋白质聚集物种，其中一些似乎是由适当纤维的结构重排形成的。
