Palladium in Chemical Protein Synthesis and Modifications
The field of site-specific modification of proteins has drawn significant attentions in recent years owing to its high importance in various research areas such as the development of novel therapeutics and understanding the biochemical and cellular behaviors of proteins. The presence of a large number of reactive functional groups in the protein of interest and in the cellular environment renders the particular modification at a specific site a highly challenging task. However, with the development of sophisticated chemical methodologies it is now possible to target a specific site of a protein with a desired modification despite many challenges remain to be solved. In this context, transition metals in particular palladium mediated C-C bond forming and C-O bond cleavage reactions gained great interest owing to the unique catalytic properties of palladium. Palladium chemistry is being significantly explored for protein modifications in vitro, on cell surface and in cellular context. Very recently, palladium complexes have been also applied for the rapid deprotection of several widely utilized cysteine-protecting groups as well as in the removal of solubilizing tags to facilitate chemical protein synthesis. This minireview highlights these advances and how the accumulated knowledge of palladium chemistry in small molecules is being impressively transferred to the area of chemical protein synthesis and modification.
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