35356-70-8Relevant articles and documents
Synthesis of water-soluble hypervalent iodine reagents for fluoroalkylation of biological thiols
Klimánková, Iveta,Hubálek, Martin,Matou?ek, Václav,Beier, Petr
supporting information, p. 10097 - 10102 (2019/12/23)
New open-chain and water-soluble hypervalent iodine reagents were synthesized and used for the transfer of fluoroalkyl groups to sulfur atoms of cysteine and cysteine-containing peptides under biocompatible conditions. Some of the reagents displayed excellent reactivity despite their limited stability in aqueous media. In reactions with a short cysteine-containing peptide, in addition to the expected S-fluoroalkylated product, a range of side-products were obtained. The amount of side-products depended on the conditions used (type of reagent, concentration, and pH). With highly activated hypervalent iodine reagents, a new reactive mode was observed-reaction with disulfides to form fluoroalkyl thiols.
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.
Reversible and diastereospecific olefin insertion into a cluster Ru-H unit. Formation of metallacycles with tertiary carbon-ruthenium σ bonds
Mani, Darjusch,Schacht, Hans-Thomas,Powell, Anne,Vahrenkamp, Heinrich
, p. 1360 - 1361 (2008/10/08)
The chiral hydrido metal clusters (μ3-RC)Ru-CoMCp(CO)8H with R = Me or Ph and M = Mo or W react reversibly with the prochiral alanine precursor acetamido acrylic acid methyl ester according to a Markownikow-type insertion of the X2C=CH2 substrate into a Ru-H bond. The cluster products formed consist of only one pair of the possible diastereoisomers rendering the reaction diastereospecific. The resulting σ-alkyl cluster complexes contain a Ru-C-N-C-O metallacycle with a tertiary carbon atom bound to ruthenium.