期刊
CHEMBIOCHEM
卷 10, 期 6, 页码 959-969出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200900002
关键词
allyl sulfides; aqueous chemistry; olefin metathesis; protein modifications; unnatural amino acids
资金
- EPSRC
- Rhodes Trust
- BBSRC [BB/E004350/1] Funding Source: UKRI
- EPSRC [EP/E000614/1, EP/G026688/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [EGA17763, BB/C510824/1, BB/E004350/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/D023335/1, GR/T26542/01, EP/E000614/1, EP/D023343/1, EP/G026688/1] Funding Source: researchfish
For a reaction to be generally useful for protein modification, it must be site-selective and efficient under conditions compatible with proteins: aqueous media, low to ambient temperature, and at or near neutral pH. To engineer a reaction that satisfies these conditions is not a simple task. Olefin metathesis is one of most useful reactions for carbon-carbon bond formation, but does it fit these requirements? This minireview is an account of the development of olefin metathesis for protein modification. Highlighted below are examples of olefin metathesis in peptidic systems and in aqueous media that laid the groundwork for successful metathesis on protein substrates. Also discussed are the opportunities in protein engineering for the genetic introduction of amino acids suitable for metathesis and the related challenges in chemistry and biology.
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