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|Title:||Site-specific covalent labeling of proteins inside live cells using small molecule probes||Authors:||Chattopadhaya, S.
In vivo protein labeling
Native chemical ligation
|Issue Date:||1-Feb-2009||Citation:||Chattopadhaya, S., Srinivasan, R., Yeo, D.S.Y., Chen, G.Y.J., Yao, S.Q. (2009-02-01). Site-specific covalent labeling of proteins inside live cells using small molecule probes. Bioorganic and Medicinal Chemistry 17 (3) : 981-989. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bmc.2008.01.043||Abstract:||The study of dynamic movement and interactions of proteins inside living cells in real time is critical for a better understanding of cellular mechanisms and functions in molecular detail. Genetically encoded fusions to fluorescent protein(s) (FP) have been widely used for this purpose [Annu. Rev. Biochem. 1998, 67, 509-544]. To obviate some of the drawbacks associated with the use of FPs [Curr. Opin. Biotechnol. 2005, 16, 1-6; Nat. Methods 2006, 3, 591-596], we report a small molecule-based approach that exploits the unique reactivity between the cysteine residue at the N-terminus of a target protein and cell-permeable, thioester-based small molecule probes resulting in site-specific, covalent tagging of proteins. This approach has been demonstrated by the in vivo labeling of proteins in both bacterial and mammalian systems thereby making it potentially useful for future bioimaging applications. © 2008 Elsevier Ltd. All rights reserved.||Source Title:||Bioorganic and Medicinal Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/76991||ISSN:||09680896||DOI:||10.1016/j.bmc.2008.01.043|
|Appears in Collections:||Staff Publications|
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