ArticleJournal of the American Chemical Society2014
SpyAvidin hubs enable precise and ultrastable orthogonal nanoassembly.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Ready-to-load MHC-I nanoparticles for high-throughput T cell screening studies.Science advances · 2026Article
- Modular Assembly of Dynamic Polymer Networks From Heteroaffinity Cross-Links to Multivalent Proteins.Angewandte Chemie (International ed. in English) · 2026Article
- A Tetrameric Biotin-Avidin Scaffold Using Anti-CD19 (FMC63) Traptavidin Fusion Enables High-Avidity CAR-T Cells for Leukemia Therapy.Bioconjugate chemistry · 2026Article
- Click biology highlights the opportunities from reliable biological reactions.Nature chemical biology · 2025Review
- Design of light- and chemically responsive protein assemblies through host-guest interactions.Chem · 2025Article
- Heme-substituted protein assembly bridged by synthetic porphyrin: achieving controlled configuration while maintaining rotational freedom.RSC advances · 2024Article
- Profibrogenic macrophage-targeted delivery of mitochondrial protector via exosome formula for alleviating pulmonary fibrosis.Bioactive materials · 2024Article
- Stable kinetochore-microtubule attachment requires loop-dependent Ndc80-Ndc80 binding.The EMBO journal · 2023Article
- Strain stiffening of Ndc80 complexes attached to microtubule plus ends.Biophysical journal · 2022Article
- Non-Covalently Associated Streptavidin Multi-Arm Nanohubs Exhibit Mechanical and Thermal Stability in Cross-Linked Protein-Network Materials.Biomacromolecules · 2022Article
- Programmable protein topology via SpyCatcher-SpyTag chemistry in one-pot cell-free expression system.Protein science : a publication of the Protein Society · 2022Article
- Protein Nanoparticles: Uniting the Power of Proteins with Engineering Design Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
- Controlled and Stable Patterning of Diverse Inorganic Nanocrystals on Crystalline Two-Dimensional Protein Arrays.Biochemistry · 2021Article
- Power to the protein: enhancing and combining activities using the Spy toolbox.Chemical science · 2020Review
- Generation of biparatopic antibody through two-step targeting of fragment antibodies on antigen using SpyTag and SpyCatcher.Biotechnology reports (Amsterdam, Netherlands) · 2020Article
- Article
- A generic cell surface ligand system for studying cell-cell recognition.PLoS biology · 2019Article
- Spy&Go purification of SpyTag-proteins using pseudo-SpyCatcher to access an oligomerization toolbox.Nature communications · 2019Article
- Ferritin-based drug delivery systems: Hybrid nanocarriers for vascular immunotargeting.Journal of controlled release : official journal of the Controlled Release Society · 2018Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The capture of biotin by streptavidin is an inspiration for supramolecular chemistry and a central tool for biological chemistry and nanotechnology, because of the rapid and exceptionally stable interaction. However, there is no robust orthogonal interaction to this hub, limiting the size and complexity of molecular assemblies that can be created. Here we combined traptavidin (a streptavidin variant maximizing biotin binding strength) with an orthogonal irreversible interaction. SpyTag is a peptide engineered to form a spontaneous isopeptide bond to its protein partner SpyCatcher. SpyTag or SpyCatcher was successfully fused to the C-terminus of Dead streptavidin subunits. We were able to generate chimeric tetramers with n (0 ≤ n ≤ 4) biotin binding sites and 4-n SpyTag or SpyCatcher binding sites. Chimeric SpyAvidin tetramers bound precise numbers of ligands fused to biotin or SpyTag/SpyCatcher. Mixing chimeric tetramers enabled assembly of SpyAvidin octamers (8 subunits) or eicosamers (20 subunits). We validated assemblies using electrophoresis and native mass spectrometry. Eicosameric SpyAvidin was used to cluster trimeric major histocompatibility complex (MHC) class I:β2-microglobulin:peptide complexes, generating an assembly with up to 56 components. MHC eicosamers surpassed the conventional MHC tetramers in acting as a powerful stimulus to T cell signaling. Combining ultrastable noncovalent with irreversible covalent interaction, SpyAvidins enable a simple route to create robust nanoarchitectures.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.