Intracellular artificial supramolecules based on de novo designed Y15 peptides
Takayuki Miki (),
Taichi Nakai,
Masahiro Hashimoto,
Keigo Kajiwara,
Hiroshi Tsutsumi and
Hisakazu Mihara
Additional contact information
Takayuki Miki: Tokyo Institute of Technology
Taichi Nakai: Tokyo Institute of Technology
Masahiro Hashimoto: Tokyo Institute of Technology
Keigo Kajiwara: Tokyo Institute of Technology
Hiroshi Tsutsumi: Tokyo Institute of Technology
Hisakazu Mihara: Tokyo Institute of Technology
Nature Communications, 2021, vol. 12, issue 1, 1-11
Abstract:
Abstract 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.
Date: 2021
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/s41467-021-23794-6 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23794-6
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-021-23794-6
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().