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Cross-dressing proteins by olefin metathesis

Nature Chemical Biology volume 4, pages 527–528 (2008)Cite this article

Chemists have established numerous methods for performing protein conjugations, but metathesis catalysts have largely remained absent from this toolkit. Evidence that proteins bearing allylsulfides undergo cross-metathesis with chosen alkenes in aqueous conditions will allow chemists to harness the power of metathesis catalysts for modifying biomolecules and other water-soluble compounds.

The covalent modification of biopolymers in living systems typically occurs with extraordinary chemoselectivity and regioselectivity. These reactions allow nature to 'accessorize' biopolymers at precise sites with an array of chemical functionalities that may be absent in the limited repertoire of monomer units available to the biosynthetic machinery. Bioorganic chemists have been remarkably successful in establishing efficient synthetic protocols for standard biopolymer chains. The current challenges are to emulate the precision with which nature performs conjugation reactions and to create artificial macromolecular structures not offered by the natural biosynthetic machinery. Two recent manuscripts1,2 from Davis et al. outline new approaches for decorating proteins with chosen appendages. Significantly, their work expands protein modification reactions to include olefin metathesis.

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Figure 1: Two approaches for site-specifically adorning proteins with desired functionalities.

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  1. Kent Kirshenbaum and Paramjit S. Arora are in the Department of Chemistry, New York University, 100 Washington Square East, New York, New York 10003, USA. kent@nyu.edu or arora@nyu.edu,

    Kent Kirshenbaum & Paramjit S Arora

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  1. Kent Kirshenbaum
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  2. Paramjit S Arora
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Kirshenbaum, K., Arora, P. Cross-dressing proteins by olefin metathesis. Nat Chem Biol 4, 527–528 (2008). https://doi.org/10.1038/nchembio0908-527

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