Tokyo Institute of Technology · Biochemistry, Genetics and Molecular Biology
Professor Takayuki Miki's research lab specializes in the design and application of de novo self-assembling peptides for synthetic biology and biomedical engineering. The lab focuses on creating peptide-based nanostructures—such as β-sheet fibrils and amyloid-like assemblies—that can form functional protein assemblies or artificial condensates inside living cells. By leveraging sequence-structure relationships and proximity labeling techniques, the lab develops tools to study protein clustering, intracellular organization, and dynamic biomolecular interactions in a controlled manner. Their work bridges peptide engineering, live-cell imaging, and systems biology to advance synthetic biomaterials and cellular engineering.
Figures are computed from collected data and may differ slightly.
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 assem
Protein assemblies forming nano- to micro-sized structures underlie versatile biological events in living systems. For mimicking and engineering these protein assemblies through a bottom-up approach, self-assembling peptides (SAPs) that form nanofibril structures via β-sheets serve as potential practical tags. Nevertheless, the development of SAP tags is still in its infancy, and insight into the relationship between peptide sequences and intracellular self-assembly is limited. In this study, we
Phage display is the most widely used technique to discover <i>de novo</i> peptides that bind to target proteins. However, it is associated with some challenges such as compositional bias. In this study, to overcome these difficulties, we devised a 'pattern enrichment analysis.' In this method, two samples (one obtained by affinity selection, the other simply amplified without selection) are prepared, and the two sequence datasets read on next-generation sequencer are compared to find the three-
In mammalian cells, protein condensates underlie diverse cell functions. Intensive synthetic biological research has been devoted to fabricating liquid droplets using de novo peptides/proteins designed from scratch in test tubes or bacterial cells. However, the development of de novo sequences for synthetic droplets forming in eukaryotes is challenging. Here, we report YK peptides, comprising 9-15 residues of alternating repeats of tyrosine and lysine, which form reversible amyloid-like fibrils
Self-assembling peptides (SAPs) are valuable building blocks for the fabrication of artificial supramolecules. We developed a guide-tag system that concentrates client proteins into SAP-based scaffolds in cellular environments at various enrichment levels. This system provides a tool to analyse the protein-protein interactions caused by protein clustering in cells.
Protein clustering is a ubiquitous event in diverse cellular processes. Self-association of proteins triggers recruitment of downstream proteins to regulate cellular signaling. To investigate the interactions in detail, chemical biology tools to identify proteins recruited to defined assemblies are required. Here, we exploit an identification of proteins recruited in artificial granules (IPRAG) platform that combines intracellular Y15-based supramolecule construction with a proximity labeling me
In mammalian cells, protein condensates underlie diverse cell functions. Intensive synthetic biological research has been devoted to fabricating liquid droplets using de novo peptides/proteins designed from scratch in test tubes or bacterial cells. However, the development of de novo sequences for synthetic droplets forming in eukaryotes is challenging. Here, we report YK peptides, comprising 9–15 residues of alternating repeats of tyrosine and lysine, which form reversible amyloid-like fibrils
Protein droplet formation is a crucial process involved in transient cellular responses and pathogenic protein aggregations. Conventionally, the droplet-forming capability of target proteins has been evaluated through <i>in vitro</i> reconstitution studies, where purified proteins are dissolved in buffer solutions. However, such droplets are highly sensitive to environmental factors, including temperature, ionic strength, and molecular crowding. Therefore, <i>in situ</i> evaluation within living
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