School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Kanagawa, Japan.
Nat Commun. 2021 Jun 7;12(1):3412. doi: 10.1038/s41467-021-23794-6.
De novo designed self-assembling peptides (SAPs) are promising building blocks of supramolecular biomaterials, which can fulfill a wide range of applications, such as scaffolds for tissue culture, three-dimensional cell culture, and vaccine adjuvants. Nevertheless, the use of SAPs in intracellular spaces has mostly been unexplored. Here, we report a self-assembling peptide, Y15 (YEYKYEYKYEYKYEY), which readily forms β-sheet structures to facilitate bottom-up synthesis of functional protein assemblies in living cells. Superfolder green fluorescent protein (sfGFP) fused to Y15 assembles into fibrils and is observed as fluorescent puncta in mammalian cells. Y15 self-assembly is validated by fluorescence anisotropy and pull-down assays. By using the Y15 platform, we demonstrate intracellular reconstitution of Nck assembly, a Src-homology 2 and 3 domain-containing adaptor protein. The artificial clusters of Nck induce N-WASP (neural Wiskott-Aldrich syndrome protein)-mediated actin polymerization, and the functional importance of Nck domain valency and density is evaluated.
从头设计的自组装肽(SAPs)是超分子生物材料有前途的构建模块,可满足广泛的应用,如组织培养、三维细胞培养和疫苗佐剂的支架。然而,SAP 在细胞内空间的应用大多尚未得到探索。在这里,我们报告了一种自组装肽 Y15(YEYKYEYKYEYKYEY),它很容易形成β-折叠结构,以促进功能性蛋白质组装在活细胞中的自下而上合成。与 Y15 融合的超折叠绿色荧光蛋白(sfGFP)组装成原纤维,并在哺乳动物细胞中观察到荧光点状结构。通过荧光各向异性和下拉测定验证了 Y15 的自组装。通过使用 Y15 平台,我们展示了 Nck 组装、Src 同源性 2 和 3 结构域包含衔接蛋白的细胞内重建。Nck 的人工簇诱导 N-WASP(神经 Wiskott-Aldrich 综合征蛋白)介导的肌动蛋白聚合,并且评估了 Nck 结构域价数和密度的功能重要性。