New protein structures can be created using a process called tag and modify, suggest UK scientists. They hope the process will lead to developments such as new drugs and biochemical probes.   

Ben Davis at the University of Oxford and his team tagged a protein with an amino acid to make a structure that can be transformed into new proteins in a Nobel Prize-winning reaction called olefin cross metathesis. This carbon-carbon double bond forming process is an important transformation reaction in organic chemistry with a broad spectrum of use, explains Davis, but until their work last year no one knew how to apply it to proteins.¹    

The team investigated different allylation pathways to incorporate a modified form of the cysteine amino acid, called S-allyl cysteine, into proteins. Davis explains that having complementary ways to incorporate the tag will widen the scope for cross metathesis in protein modification.    

Robert Grubbs from the California Institute of Technology, Pasadena, US, who shared the 2005 Nobel Prize in chemistry, in particular for his contribution to work on the metathesis reaction, says that Davis' method is excellent. 'It demonstrates a new technique for protein modification with a wide array of functionality,' he adds.   

There are many possibilities for using cross metathesis to form new protein structures, says Davis. For example, ring-closing cross metathesis could be used to stabilise large structures like enzymes, he suggests.  'Ultimately, we believe we can use a panel of tags and reactions to modify to re-programme protein structure and function at will, simply using chemistry,' he says. David Crich, an expert in carbohydrate synthesis at The National Centre for Scientific Research, Gif-sur-Yvette, France, comments: 'This combination of direct allylation and subsequent metathesis is sure to find widespread application.'   

Katherine Davies 

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