Dong He, Paramonov Sergey E, Hartgerink Jeffrey D
Department of Chemistry, Rice University, 6100 Main Street, Mail Stop 60, Houston, Texas 77005, USA.
J Am Chem Soc. 2008 Oct 15;130(41):13691-5. doi: 10.1021/ja8037323. Epub 2008 Sep 20.
The alpha-helical coiled coil is one of the best-studied and most well-understood protein folding motifs. In particular, the coiled coil can be made to self-assemble into a nanofibrous architecture with many potential applications in biomimetic engineering and elsewhere. The key to the assembly of such nanofibers has been the formation of "sticky ended" dimers through careful selection of electrostatically charged amino acids. In this work, we demonstrate for the first time that sticky ended dimers are not a prerequisite for alpha-helical coiled coil nanofiber formation. In contrast, we show that blunt-ended dimers are able to form nanofibers with a uniform diameter of 4 nm while being hundreds of nanometers in length. Furthermore, the length and lateral packing can be controlled through selection of amino acids not involved in the coiled coil interface.
α-螺旋卷曲螺旋是研究最为深入且理解最为透彻的蛋白质折叠基序之一。特别是,卷曲螺旋能够自组装成纳米纤维结构,在仿生工程及其他领域具有诸多潜在应用。此类纳米纤维组装的关键在于通过精心选择带静电的氨基酸形成“粘性末端”二聚体。在这项工作中,我们首次证明粘性末端二聚体并非α-螺旋卷曲螺旋纳米纤维形成的先决条件。相反,我们表明平头二聚体能够形成直径均匀为4纳米、长度达数百纳米的纳米纤维。此外,通过选择不参与卷曲螺旋界面的氨基酸,可以控制纳米纤维的长度和侧向堆积。