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Biocompatible Copper(I) Catalysts for in Vivo Imaging of Glycans

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Department of Biochemistry and Developmental and Molecular Biology, Albert Einstein College of Medicine, Yeshiva University, 1300 Morris Park Ave, Bronx, New York 10461, United States, and The Molecular Foundry, Lawrence Berkeley National Laboratory, One Cyclotron Road, MS 67R6110, Berkeley, California 94720, United States
[email protected]
†Department of Biochemistry, Albert Einstein College of Medicine, Yeshiva University.
#Developmental and Molecular Biology, Albert Einstein College of Medicine, Yeshiva University.
‡The Molecular Foundry, Lawrence Berkeley National Laboratory.
Cite this: J. Am. Chem. Soc. 2010, 132, 47, 16893–16899
Publication Date (Web):November 9, 2010
https://doi.org/10.1021/ja106553e
Copyright © 2010 American Chemical Society
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    Abstract

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    The Cu(I)-catalyzed azide−alkyne cycloaddition (CuAAC) is the standard method for bioorthogonal conjugation. However, current Cu(I) catalyst formulations are toxic, hindering their use in living systems. Here we report that BTTES, a tris(triazolylmethyl)amine-based ligand for Cu(I), promotes the cycloaddition reaction rapidly in living systems without apparent toxicity. This catalyst allows, for the first time, noninvasive imaging of fucosylated glycans during zebrafish early embryogenesis. We microinjected embryos with alkyne-bearing GDP-fucose at the one-cell stage and detected the metabolically incorporated unnatural sugars using the biocompatible click chemistry. Labeled glycans could be imaged in the enveloping layer of zebrafish embryos between blastula and early larval stages. This new method paves the way for rapid, noninvasive imaging of biomolecules in living organisms.

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    Synthetic procedures, spectral data for BTTES, protocol for kinetic measurement, experimental procedures for flow cytometry, fluorescent microscopy, and zebrafish husbandry and strains. This material is available free of charge via the Internet at http://pubs.acs.org.

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    80. Hanqing Zhao, Yuelan He, Yingtung Lo, Huizhu Song, Jianzhong Lu. Fluorescent probes based on bioorthogonal reactions: Construction strategies and applications. TrAC Trends in Analytical Chemistry 2023, 169 , 117388. https://doi.org/10.1016/j.trac.2023.117388
    81. Daniel J. Stone, Miguel Macias-Contreras, Shaun M. Crist, Christelle F. T. Bucag, Gwimoon Seo, Lei Zhu. SNAP-tagging live cells via chelation-assisted copper-catalyzed azide–alkyne cycloaddition. Organic & Biomolecular Chemistry 2023, 21 (36) , 7419-7436. https://doi.org/10.1039/D3OB01003A
    82. Kutloano Edward Sekhosana, Shereen A. Majeed, Usisipho Feleni. Click chemistry in the electrochemical systems: Toward the architecture of electrochemical (bio)sensors. Coordination Chemistry Reviews 2023, 491 , 215232. https://doi.org/10.1016/j.ccr.2023.215232
    83. Sijun Pan, Aixiang Ding, Yisi Li, Yaxin Sun, Yueqin Zhan, Zhenkun Ye, Ning Song, Bo Peng, Lin Li, Wei Huang, Huilin Shao. Small-molecule probes from bench to bedside: advancing molecular analysis of drug–target interactions toward precision medicine. Chemical Society Reviews 2023, 52 (16) , 5706-5743. https://doi.org/10.1039/D3CS00056G
    84. Jianbo Li, Xuepu Feng, Wenting Wang, Mengbi Guo, Jing Yang, Xiang Li, Rui Yang, Bo Yang. Cyclodextrin-based multifunctional supramolecular catalysts for aqueous CuAAC reaction. Applied Catalysis A: General 2023, 663 , 119309. https://doi.org/10.1016/j.apcata.2023.119309
    85. Adam D. Moorhouse, Joshua A. Homer, John E. Moses. The certainty of a few good reactions. Chem 2023, 9 (8) , 2063-2077. https://doi.org/10.1016/j.chempr.2023.03.017
    86. Roy A. J. F. Oerlemans, Jingxin Shao, Sander G. A. M. Huisman, Yudong Li, Loai K. E. A. Abdelmohsen, Jan C. M. van Hest. Compartmentalized Intracellular Click Chemistry with Biodegradable Polymersomes. Macromolecular Rapid Communications 2023, 44 (16) https://doi.org/10.1002/marc.202200904
    87. Christin Bednarek, Ute Schepers, Franziska Thomas, Stefan Bräse. Bioconjugation in Materials Science. Advanced Functional Materials 2023, 1 https://doi.org/10.1002/adfm.202303613
    88. T. Moritz Weber, Jörg Pietruszka. Synthesis of a Water-Soluble Tridentate (Dimethylamino)ethyl Cu(I)/Cu(II)-Ligand. Synthesis 2023, 55 (14) , 2128-2133. https://doi.org/10.1055/a-2034-9427
    89. Madonna M. A. Mitry, Francesca Greco, Helen M. I. Osborn. In Vivo Applications of Bioorthogonal Reactions: Chemistry and Targeting Mechanisms. Chemistry – A European Journal 2023, 29 (20) https://doi.org/10.1002/chem.202203942
    90. Lan Lin, Lai Jiang, En Ren, Gang Liu. Bioorthogonal chemistry based on-demand drug delivery system in cancer therapy. Frontiers of Chemical Science and Engineering 2023, 17 (4) , 483-489. https://doi.org/10.1007/s11705-022-2227-2
    91. Bing Gao. Making functional connections: A summary of the Nobel Prize in Chemistry 2022. Chinese Science Bulletin 2022, 67 (36) , 4332-4336. https://doi.org/10.1360/TB-2022-1201
    92. Pascal Hoffmann, Christian Lherbet, Isabelle Fabing, Marie-Claire Barthélémy, Yann Borjon-Piron, Christophe Laurent, Alain Vigroux. A mesoporous metal–organic framework used to sustainably release copper( ii ) into reducing aqueous media to promote the CuAAC click reaction. RSC Advances 2022, 12 (41) , 26825-26833. https://doi.org/10.1039/D2RA04298C
    93. Andrés Seoane, José Luis Mascareñas. Exporting Homogeneous Transition Metal Catalysts to Biological Habitats. European Journal of Organic Chemistry 2022, 2022 (32) https://doi.org/10.1002/ejoc.202200118
    94. Yifei Liu, Ka Lun Lai, Kenward Vong. Transition Metal Scaffolds Used To Bring New‐to‐Nature Reactions into Biological Systems. European Journal of Inorganic Chemistry 2022, 2022 (21) https://doi.org/10.1002/ejic.202200215
    95. Endri Karaj, Shaimaa H. Sindi, L.M. Viranga Tillekeratne. Photoaffinity labeling and bioorthogonal ligation: Two critical tools for designing “Fish Hooks” to scout for target proteins. Bioorganic & Medicinal Chemistry 2022, 62 , 116721. https://doi.org/10.1016/j.bmc.2022.116721
    96. Zongyang Li, Yaxuan Li, Wenxu Chang, Sen Pang, Xuefeng Li, Liusheng Duan, Zhenhua Zhang. Synthesis and Fluorescent Properties of Aminopyridines and the Application in “Click and Probing”. Molecules 2022, 27 (5) , 1596. https://doi.org/10.3390/molecules27051596
    97. Thao M. Xiong, Edzna S. Garcia, Junfeng Chen, Lingyang Zhu, Ariale J. Alzona, Steven C. Zimmerman. Enzyme-like catalysis by single chain nanoparticles that use transition metal cofactors. Chemical Communications 2022, 58 (7) , 985-988. https://doi.org/10.1039/D1CC05578J
    98. Hongjie Xiong, Liu Liu, Yihan Wang, Hui Jiang, Xuemei Wang. Engineered Aptamer‐Organic Amphiphile Self‐Assemblies for Biomedical Applications: Progress and Challenges. Small 2022, 18 (4) https://doi.org/10.1002/smll.202104341
    99. Samuel L. Scinto, Didier A. Bilodeau, Robert Hincapie, Wankyu Lee, Sean S. Nguyen, Minghao Xu, Christopher W. am Ende, M. G. Finn, Kathrin Lang, Qing Lin, John Paul Pezacki, Jennifer A. Prescher, Marc S. Robillard, Joseph M. Fox. Bioorthogonal chemistry. Nature Reviews Methods Primers 2021, 1 (1) https://doi.org/10.1038/s43586-021-00028-z
    100. Zilong Li, Qinhua Chen, Jin Wang, Xiaoyan Pan, Wen Lu. Research Progress and Application of Bioorthogonal Reactions in Biomolecular Analysis and Disease Diagnosis. Topics in Current Chemistry 2021, 379 (6) https://doi.org/10.1007/s41061-021-00352-8
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