Sunday, February 6, 2011
Cholesterol & protein studied by Click chemistry
Chemical Communications Received 31st October 2010, Accepted 21st December 2010 DOI: 10.1039/c0cc04710d
Tate and coworkers from Imperial College London reported the bioorthogonal click chemistry of a fluorescent alkyne probe with azido-modified post-translationally cholesterylated proteins - in living cells. The design is shown in the drawing. This enables rapid multiplexed fluorescence detection and affinity labelling of protein cholesterylation. This method, in comparison with the current radiolabeling, offers safety, speed, sensitivity, and flexibility. It may allow the observation of protein cholesterylation over space and time using fluorescence microscopy.
In more complex and challenging environment, click chemistry has found application and success, only due to its extremely high efficiency and orthogonality.