1184775-97-0Relevant academic research and scientific papers
Synthesis of selenium-containing bicyclic β-lactams via alkene metathesis
Garud, Dinesh R.,Garud, Deepali D.,Koketsu, Mamoru
, p. 2591 - 2598 (2009)
The stereoselective insertion of allyl-seleno moieties at the C(4) position of azetidinones and further ring-closing metathesis afforded novel selenium-containing bicyclic β-lactams. The Royal Society of Chemistry 2009.
Rapid cross-metathesis for reversible protein modifications via chemical access to se-allyl-selenocysteine in proteins
Lin, Yuya A.,Boutureira, Omar,Lercher, Lukas,Bhushan, Bhaskar,Paton, Robert S.,Davis, Benjamin G.
supporting information, p. 12156 - 12159 (2013/09/23)
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.
