We thank Carolyn Kwa, Daniel Liu, and Ken Loh for assistance with neuron culture, Jennifer Yao for LplA enzymes, and Peng Zou for critical reading of the manuscript. Prof. M. G. Finn (Scripps) provided the initial batch of THPTA ligand. Funding was provided by the NIH (R01 GM072670), the Dreyfus Foundation, and the American Chemical Society. C.U. was supported by the C.P. Chu and Y. Lai summer graduate fellowship (MIT).
Zuschrift
Fast, Cell-Compatible Click Chemistry with Copper-Chelating Azides for Biomolecular Labeling†
Article first published online: 3 MAY 2012
DOI: 10.1002/ange.201108181
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Uttamapinant, C., Tangpeerachaikul, A., Grecian, S., Clarke, S., Singh, U., Slade, P., Gee, K. R. and Ting, A. Y. (2012), Fast, Cell-Compatible Click Chemistry with Copper-Chelating Azides for Biomolecular Labeling. Angew. Chem., 124: 5954–5958. doi: 10.1002/ange.201108181
- †
Publication History
- Issue published online: 5 JUN 2012
- Article first published online: 3 MAY 2012
- Manuscript Revised: 13 FEB 2012
- Manuscript Received: 21 NOV 2011
Funded by
- NIH. Grant Number: R01 GM072670
- Dreyfus Foundation
- American Chemical Society
Keywords:
- Fluoreszenzsonden;
- Klick-Chemie;
- Liponsäureligase;
- Metabolische Markierung;
- Protein-Engineering

Kupfer-chelatisierende Azide reagieren unter biokompatiblen Bedingungen sehr viel schneller in Klick-Reaktionen (CuAAC) als nichtchelatisierende Azide. Damit gelingt es, Proteine an der Oberfläche lebender Zellen mit nur 10–40 μM CuI/CuII ortsspezifisch zu markieren (siehe Schema). Auch die Empfindlichkeit für den CuAAC-basierten Nachweis Alkin-modifizierter Proteine und RNA wird gesteigert.

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