Probing small molecule binding to amyloid fibrils
Probing small molecule binding to amyloid fibrils
复制标题
DOI：
10.1039/c1cp22283j
复制
发表时间：
2011-01-01
影响因子：
3.3
通讯作者：
Knowles, Tuomas P. J.
中科院分区：
文献类型：
--
作者：
Buell, Alexander K.;Esbjoerner, Elin K.;Knowles, Tuomas P. J.
近年来，许多努力集中在探索小分子与淀粉样纤维和其他蛋白质聚集体的相互作用上。理解和控制这种相互作用对于在蛋白质聚集与疾病相关的情况下开发诊断和治疗策略是重要的。在这篇透视文章中，我们概述了用于研究淀粉样蛋白-小分子相互作用的生物物理方法的工具箱。我们详细讨论了两个最近开发的技术在这个框架内：线性二色性，更传统的光谱技术的一个有前途的扩展，和生物传感方法，其中表面结合的淀粉样蛋白纤维暴露于小分子的解决方案。这两种技术都依赖于测量与小分子与淀粉样蛋白聚集体的结合非常直接相关的物理性质，因此提供了一种有吸引力的途径来探测这些重要的相互作用。
Much effort has focussed in recent years on probing the interactions of small molecules with amyloid fibrils and other protein aggregates. Understanding and control of such interactions are important for the development of diagnostic and therapeutic strategies in situations where protein aggregation is associated with disease. In this perspective article we give an overview over the toolbox of biophysical methods for the study of such amyloid-small molecule interactions. We discuss in detail two recently developed techniques within this framework: linear dichroism, a promising extension of the more traditional spectroscopic techniques, and biosensing methods, where surface-bound amyloid fibrils are exposed to solutions of small molecules. Both techniques rely on the measurement of physical properties that are very directly linked to the binding of small molecules to amyloid aggregates and therefore provide an attractive route to probe these important interactions.