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Chemical biology

Protein modification in a trice

Nature volume 526, pages 646–647 (2015)Cite this article

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Organometallic reagents have been developed that chemically modify proteins and peptides specifically at cysteine amino-acid residues — potentially offering a general route to making therapeutically useful compounds. See Letter p.687

Proteins are valuable therapeutic and imaging agents, but they often need to be chemically modified to work optimally in these roles. If a protein is to remain fully biologically active after a chemical group has been attached, the modification must often take place at a specific, predetermined amino-acid side chain. On page 687 of this issue, Vinogradova et al.1 report palladium-containing organometallic reagents that not only modify proteins and peptides at selective sites, but also do so quickly and without being heated, to generate high yields of products.

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Figure 1: Site-selective reactions with proteins.

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Authors and Affiliations

  1. Heather Maynard is in the Department of Chemistry and Biochemistry and the California NanoSystems Institute, University of California, Los Angeles, Los Angeles, California 90095, USA.,

    Heather Maynard

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  1. Heather Maynard
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Correspondence to Heather Maynard.

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Maynard, H. Protein modification in a trice. Nature 526, 646–647 (2015). https://doi.org/10.1038/526646b

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