The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Secrets of a covalent interaction for biomaterials and biotechnology: SpyTag and SpyCatcher
Open accessAbstract
SpyTag is a short peptide that forms an isopeptide bond upon encountering its protein partner SpyCatcher. This covalent peptide interaction is a simple and powerful tool for bioconjugation and extending what protein architectures are accessible. Here we review the origin and mechanism of SpyTag/SpyCatcher, focusing on recent innovative applications. Ligation of targeting-antibody with antigen provided a simple route to vaccine generation. SpyRings, from head-to-tail cyclisation, gave major enhancements in enzyme resilience. Linking multiple SpyCatchers gave dendrimers for T-cell activation or Spy networks forming hydrogels for stem cell culture. Synthetic biology applications include integrating amyloid biomaterials with living bacteria, for irreversible derivatisation of biofilms with enzymes or nanoparticles. We also discuss further opportunities to apply and enhance SpyTag/SpyCatcher technology.
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Cites
Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin
Zakeri, B., Fierer, J. O., Celik, E., Chittock, E. C., Schwarz-Linek, U., Moy, V. T., & Howarth, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1115485109 · Cited by 1,662
Self-citationSite-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index
Junutula, J. R., Raab, H., Clark, S., Bhakta, S., Leipold, D. D., Weir, S., Chen, Y., Simpson, M., Tsai, S. P., Dennis, M. S., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt.1480 · Cited by 1,382
Addition of p-Azido-l-phenylalanine to the Genetic Code of Escherichia coli
Chin, J. W., Santoro, S. W., Martin, A. B., King, D. S., Wang, L., & Schultz, P. G. (2002) · Journal of the American Chemical Society · doi:10.1021/ja027007w · Cited by 721
Finding the Right (Bioorthogonal) Chemistry
Patterson, D. M., Nazarova, L. A., & Prescher, J. A. (2014) · ACS Chemical Biology · doi:10.1021/cb400828a · Cited by 652
Choosing an effective protein bioconjugation strategy
Stephanopoulos, N., & Francis, M. B. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.720 · Cited by 634
Sortase-Mediated Protein Ligation: A New Method for Protein Engineering
Mao, H., Hart, S. A., Schink, A., & Pollok, B. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039915e · Cited by 534
Lang, K., Davis, L., Wallace, S., Mahesh, M., Cox, D. J., Blackman, M. L., Fox, J. M., & Chin, J. W. (2012) · Journal of the American Chemical Society · doi:10.1021/ja302832g · Cited by 523
Lang, K., Davis, L., Torres-Kolbus, J., Chou, C., Deiters, A., & Chin, J. W. (2012) · Nature Chemistry · doi:10.1038/nchem.1250 · Cited by 487
Inteins: nature's gift to protein chemists
Shah, N. H., & Muir, T. W. (2014) · Chem. Sci. · doi:10.1039/c3sc52951g · Cited by 404
Synthesis and patterning of tunable multiscale materials with engineered cells
Chen, A. Y., Deng, Z., Billings, A. N., Seker, U. O. S., Lu, M. Y., Citorik, R. J., Zakeri, B., & Lu, T. K. (2014) · Nature Materials · doi:10.1038/nmat3912 · Cited by 379
Cited by
Liu, X., Yang, X., Yang, Z., Luo, J., Tian, X., Liu, K., Kou, S., & Sun, F. (2018) · ACS Applied Nano Materials · doi:10.1021/acsanm.8b00077 · Cited by 32
Metadata
- Authors
- Reddington, S. C., & Howarth, M.
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2015-12
- Volume
- 29
- Pages
- 94-99
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W2151007289
- Cited by
- 326
- References
- 35
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.