期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 27, 期 4, 页码 342-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41594-020-0397-5
关键词
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资金
- NIH [R01 GM123378]
- Fred Hutchinson Cancer Research Center
Circular nanoparticles self-assembled from designed tandem repeat proteins are functionalized by fusing different protein domains at defined positions and copy numbers. These constructs can activate T cells via high-avidity interactions on the cell surface. Protein engineering has enabled the design of molecular scaffolds that display a wide variety of sizes, shapes, symmetries and subunit compositions. Symmetric protein-based nanoparticles that display multiple protein domains can exhibit enhanced functional properties due to increased avidity and improved solution behavior and stability. Here we describe the creation and characterization of a computationally designed circular tandem repeat protein (cTRP) composed of 24 identical repeated motifs, which can display a variety of functional protein domains (cargo) at defined positions around its periphery. We demonstrate that cTRP nanoparticles can self-assemble from smaller individual subunits, can be produced from prokaryotic and human expression platforms, can employ a variety of cargo attachment strategies and can be used for applications (such as T-cell culture and expansion) requiring high-avidity molecular interactions on the cell surface.
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