33173-55-6Relevant articles and documents
Modular click chemistry libraries for functional screens using a diazotizing reagent
Meng, Genyi,Guo, Taijie,Ma, Tiancheng,Zhang, Jiong,Shen, Yucheng,Sharpless, Karl Barry,Dong, Jiajia
, p. 86 - 89 (2019/11/13)
Click chemistry is a concept in which modular synthesis is used to rapidly find new molecules with desirable properties1. Copper(i)-catalysed azide–alkyne cycloaddition (CuAAC) triazole annulation and sulfur(vi) fluoride exchange (SuFEx) catalysis are widely regarded as click reactions2–4, providing rapid access to their products in yields approaching 100% while being largely orthogonal to other reactions. However, in the case of CuAAC reactions, the availability of azide reagents is limited owing to their potential toxicity and the risk of explosion involved in their preparation. Here we report another reaction to add to the click reaction family: the formation of azides from primary amines, one of the most abundant functional groups5. The reaction uses just one equivalent of a simple diazotizing species, fluorosulfuryl azide6–11 (FSO2N3), and enables the preparation of over 1,200 azides on 96-well plates in a safe and practical manner. This reliable transformation is a powerful tool for the CuAAC triazole annulation, the most widely used click reaction at present. This method greatly expands the number of accessible azides and 1,2,3-triazoles and, given the ubiquity of the CuAAC reaction, it should find application in organic synthesis, medicinal chemistry, chemical biology and materials science.
Puromycin Analogues Capable of Multiplexed Imaging and Profiling of Protein Synthesis and Dynamics in Live Cells and Neurons
Ge, Jingyan,Zhang, Cheng-Wu,Ng, Xue Wen,Peng, Bo,Pan, Sijun,Du, Shubo,Wang, Danyang,Li, Lin,Lim, Kah-Leong,Wohland, Thorsten,Yao, Shao Q.
supporting information, p. 4933 - 4937 (2016/04/26)
Newly synthesized proteins constitute an important subset of the proteome involved in every cellular process, yet existing chemical tools used to study them have major shortcomings. Herein we report a suite of cell-permeable puromycin analogues capable of being metabolically incorporated into newly synthesized proteins in different mammalian cells, including neuronal cells. Subsequent labeling with suitable bioorthogonal reporters, in both fixed and live cells, enabled direct imaging and enrichment of these proteins. By taking advantage of the mutually orthogonal reactivity of these analogues, we showed multiplexed labeling of different protein populations, as well as quantitative measurements of protein dynamics by fluorescence correlation spectroscopy, could be achieved in live-cell environments. Tag and see: A suite of cell-permeable puromycin analogues that are capable of multiplexed imaging of newly synthesized proteins in live cells and neurons has been developed. For the first time, diffusion dynamics of newly synthesized proteins inside live neuron-like dendritic cells were quantitatively measured, revealing a heterogeneous behavior.
A simple quick route to fullerene amino acid derivatives
Strom, T. Amanda,Barron, Andrew R.
supporting information; experimental part, p. 4764 - 4766 (2010/09/16)
Two new fullerene amino acids have been prepared by dipolar addition to C60 of either the Boc- or Fmoc-Nα-protected azido amino acids derived from phenylalanine and lysine. UV-visible and CV studies indicate the as prepared amino acids are a mi
