Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, United Kingdom.
ACS Nano. 2013 Dec 23;7(12):10443-8. doi: 10.1021/nn406121w.
The self-assembly of protein molecules into highly ordered linear aggregates, known as amyloid fibrils, is a phenomenon receiving increasing attention because of its biological roles in health and disease and the potential of these structures to form artificial proteinaceous scaffolds for biomaterials applications. A particularly powerful approach to probe the key physical properties of fibrillar structures is atomic force microscopy, which was used by Usov et al. in this issue of ACS Nano to reveal the polymorphic transitions and chirality inversions of amyloid fibrils in unprecedented detail. Starting from this study, this Perspective highlights recent progress in understanding the dynamic polymorphism, twisting behavior, and handedness of amyloid fibrils and discusses the promising future of these self-assembling structures as advanced functional materials with applications in nanotechnology and related fields.
蛋白质分子自组装成高度有序的线性聚集体，即淀粉样纤维，这一现象因其在健康和疾病中的生物学作用以及这些结构在生物材料应用中形成人工蛋白质支架的潜力而受到越来越多的关注。原子力显微镜是一种特别强大的方法，可以探测纤维状结构的关键物理特性，Usov 等人在本期 ACS Nano 中使用原子力显微镜以前所未有的细节揭示了淀粉样纤维的多态转变和手性反转。从这项研究出发，本观点强调了理解淀粉样纤维的动态多态性、扭曲行为和手性的最新进展，并讨论了这些自组装结构作为具有纳米技术和相关领域应用的先进功能材料的广阔前景。
