期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 135, 期 33, 页码 12156-12159出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja403191g
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资金
- EPSRC
- CRUK
- Rhodes Trust
- EU
- Royal Society
- BBSRC [BB/E004350/1] Funding Source: UKRI
- EPSRC [EP/I500200/1, EP/E000614/1, EP/G026688/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/C510824/1, EGA17763, BB/E004350/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/E000614/1, GR/T26542/01, EP/D023343/1, EP/G026688/1, EP/I500200/1, EP/D023335/1] Funding Source: researchfish
Cross-metathesis (CM) has recently emerged as a viable strategy for protein modification. Here, efficient protein CM has been demonstrated through biomimetic chemical access to Se-allyl-selenocysteine (Seac), a metathesis-reactive amino acid substrate, via dehydroalanine. On-protein reaction kinetics reveal a rapid reaction with rate constants of Seac-mediated-CM comparable or superior to off-protein rates of many current bioconjugations. This use of Se-relayed Seac CM on proteins has now enabled reactions with substrates (allyl GlcNAc, N-allyl acetamide) that were previously not possible for the corresponding sulfur analogue. This CM strategy was applied to histone proteins to install a mimic of acetylated lysine (KAc, an epigenetic marker). The resulting synthetic H3 was successfully recognized by antibody that binds natural H3-K9Ac. Moreover, Cope-type selenoxide elimination allowed this putative marker (and function) to be chemically expunged, regenerating an H3 that can be rewritten to complete a chemically enabled write (CM)-erase (ox)-rewrite (CM) cycle.
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