Journal
BIOCONJUGATE CHEMISTRY
Volume 21, Issue 10, Pages 1912-1916Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bc100272z
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Funding
- NIH [R01 CA 112075, K99 EB009105]
- American Heart Association
- Skaggs Institute for Chemical Biology
- W.M. Keck Foundation
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The copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction, optimized for biological molecules in aqueous buffers, has been shown to rapidly label mammalian cells in culture with no loss in cell viability. Metabolic uptake and display of the azide derivative of N-acetylmannosamine developed by Bertozzi, followed by CuAAC ligation using sodium ascorbate and the ligand tris(hydroxypropyltriazolyl)methylamine (THPTA), gave rise to abundant covalent attachment of dye-alkyne reactants. THPTA serves both to accelerate the CuAAC reaction and to protect the cells from damage by oxidative agents produced by the Cu-catalyzed reduction of oxygen by ascorbate, which is required to maintain the metal in the active +1 oxidation state. This procedure extends the application of this fastest of azide-based bioorthogonal reactions to the exterior of living cells.
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