Bioorthogonal chemistry amplifies nanoparticle binding and enhances the sensitivity of cell detection
Source abstract
Abstract
Nanoparticles have emerged as key materials for biomedical applications because of their unique and tunable physical properties, multivalent targeting capability, and high cargo capacity. Motivated by these properties and by current clinical needs, numerous diagnostic and therapeutic nanomaterials have recently emerged. Here we describe a novel nanoparticle targeting platform that uses a rapid, catalyst-free cycloaddition as the coupling mechanism. Antibodies against biomarkers of interest were modified with trans-cyclooctene and used as scaffolds to couple tetrazine-modified nanoparticles onto live cells. We show that the technique is fast, chemoselective, adaptable to metal nanomaterials, and scalable for biomedical use. This method also supports amplification of biomarker signals, making it superior to alternative targeting techniques including avidin/biotin.
Source: europepmc · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Click Chemistry and Applications · Monoclonal and Polyclonal Antibodies Research · Advanced Biosensing Techniques and Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (30)
Show source-provided references
1. Davis, M. E., Chen, Z. G. & Shin, D. M. Nanoparticle therapeutics: an emerging treatment modality for cancer. Nature Rev. Drug Discov. 7, 771–782 (2008).10.1038/nrd2614 ↗
2. Weissleder, R. & Pittet, M. J. Imaging in the era of molecular oncology. Nature 452, 580–589 (2008).10.1038/nature06917 ↗
3. Giljohann, D. A. & Mirkin, C. A. Drivers of biodiagnostic development. Nature 462, 461–464 (2009).10.1038/nature08605 ↗
4. Choi, H. S. et al. Design considerations for tumour-targeted nanoparticles. Nature Nanotech. 5, 42–47 (2010).10.1038/nnano.2009.314 ↗
5. Jin, Y. & Gao, X. Plasmonic fluorescent quantum dots. Nature Nanotech. 4, 571–576 (2009).10.1038/nnano.2009.193 ↗
6. Chen, Z. et al. Protein microarrays with carbon nanotubes as multicolor Raman labels. Nature Biotechnol. 26, 1285–1292 (2008).10.1038/nbt.1501 ↗
7. Qian, X. et al. In vivo tumor targeting and spectroscopic detection with surface-enhanced Raman nanoparticle tags. Nature Biotechnol. 26, 83–90 (2008).10.1038/nbt1377 ↗
8. Lee, J. H. et al. Artificially engineered magnetic nanoparticles for ultra-sensitive molecular imaging. Nature Med. 13, 95–99 (2007).10.1038/nm1467 ↗
9. Gao, X., Cui, Y., Levenson, R. M., Chung, L. W. & Nie, S. In vivo cancer targeting and imaging with semiconductor quantum dots. Nature Biotechnol. 22, 969–976 (2004).10.1038/nbt994 ↗
10. Nam, J. M., Thaxton, C. S. & Mirkin, C. A. Nanoparticle-based bio-bar codes for the ultrasensitive detection of proteins. Science 301, 1884–1886 (2003).10.1126/science.1088755 ↗
11. Peer, D. et al. Nanocarriers as an emerging platform for cancer therapy. Nature Nanotech. 2, 751–760 (2007).10.1038/nnano.2007.387 ↗
12. Cho, K., Wang, X., Nie, S., Chen, Z. G. & Shin, D. M. Therapeutic nanoparticles for drug delivery in cancer. Clin. Cancer Res. 14, 1310–1316 (2008).10.1158/1078-0432.CCR-07-1441 ↗
13. Akinc, A. et al. A combinatorial library of lipid-like materials for delivery of RNAi therapeutics. Nature Biotechnol. 26, 561–569 (2008).10.1038/nbt1402 ↗
14. Shaw, S. Y. et al. Perturbational profiling of nanomaterial biologic activity. Proc. Natl Acad. Sci. USA 105, 7387–7392 (2008).10.1073/pnas.0802878105 ↗
15. Xing, Y. et al. Bioconjugated quantum dots for multiplexed and quantitative immunohistochemistry. Nature Protoc. 2, 1152–1165 (2007).10.1038/nprot.2007.107 ↗
16. Devaraj, N. K., Upadhyay, R., Haun, J. B., Hilderbrand, S. A. & Weissleder, R. Fast and sensitive pretargeted labeling of cancer cells through a tetrazine/trans-cyclooctene cycloaddition. Angew. Chem. Int. Ed. 48, 7013–7016 (2009).10.1002/anie.200903233 ↗
17. Devaraj, N. K., Weissleder, R. & Hilderbrand, S. A. Tetrazine-based cycloadditions: application to pretargeted live cell imaging. Bioconjug. Chem. 19, 2297–2299 (2008).10.1021/bc8004446 ↗
18. Blackman, M. L., Royzen, M. & Fox, J. M. Tetrazine ligation: fast bioconjugation based on inverse-electron-demand Diels–Alder reactivity. J. Am. Chem. Soc. 130, 13518–13519 (2008).10.1021/ja8053805 ↗
19. Lee, H., Sun, E., Ham, D. & Weissleder, R. Chip-NMR biosensor for detection and molecular analysis of cells. Nature Med. 14, 869–874 (2008).10.1038/nm.1711 ↗
20. Lee, H., Yoon, T. J., Figueiredo, J. L., Swirski, F. K. & Weissleder, R. Rapid detection and profiling of cancer cells in fine-needle aspirates. Proc. Natl Acad. Sci. USA 106, 12459–12464 (2009).10.1073/pnas.0902365106 ↗
21. Hudis, C. A. Trastuzumab—mechanism of action and use in clinical practice. N. Engl. J. Med. 357, 39–51 (2007).10.1056/NEJMra043186 ↗
22. Hong, K. W. et al. A novel anti-EGFR monoclonal antibody inhibiting tumor cell growth by recognizing different epitopes from cetuximab. J. Biotechnol. 145, 84–91 (2010).10.1016/j.jbiotec.2009.09.023 ↗
23. Troise, F., Cafaro, V., Giancola, C., D'Alessio, G. & De Lorenzo, C. Differential binding of human immunoagents and Herceptin to the ErbB2 receptor. FEBS J. 275, 4967–4979 (2008).10.1111/j.1742-4658.2008.06625.x ↗
24. Green, N. M. Avidin and streptavidin. Methods Enzymol. 184, 51–67 (1990).10.1016/0076-6879(90)84259-J ↗
25. Chinol, M. et al. Biochemical modifications of avidin improve pharmacokinetics and biodistribution, and reduce immunogenicity. Br. J. Cancer 78, 189–197 (1998).10.1038/bjc.1998.463 ↗
26. Nagrath, S. et al. Isolation of rare circulating tumour cells in cancer patients by microchip technology. Nature 450, 1235–1239 (2007).10.1038/nature06385 ↗
27. Maheswaran, S. et al. Detection of mutations in EGFR in circulating lung-cancer cells. N. Engl. J. Med. 359, 366–377 (2008).10.1056/NEJMoa0800668 ↗
28. Pantel, K., Brakenhoff, R. H. & Brandt, B. Detection, clinical relevance and specific biological properties of disseminating tumour cells. Nature Rev. Cancer 8, 329–340 (2008).10.1038/nrc2375 ↗
29. Reynolds, F., O'Loughlin, T., Weissleder, R. & Josephson, L. Method of determining nanoparticle core weight. Anal. Chem. 77, 814–817 (2005).10.1021/ac049307x ↗
30. Piran, U. & Riordan, W. J. Dissociation rate constant of the biotin–streptavidin complex. J. Immunol. Methods 133, 141–143 (1990).10.1016/0022-1759(90)90328-S ↗