Light-driven post-translational installation of reactive protein side chains was written by Josephson, Brian;Fehl, Charlie;Isenegger, Patrick G.;Nadal, Simon;Wright, Tom H.;Poh, Adeline W. J.;Bower, Ben J.;Giltrap, Andrew M.;Chen, Lifu;Batchelor-McAuley, Christopher;Roper, Grace;Arisa, Oluwatobi;Sap, Jeroen B. I.;Kawamura, Akane;Baldwin, Andrew J.;Mohammed, Shabaz;Compton, Richard G.;Gouverneur, Veronique;Davis, Benjamin G.. And the article was included in Nature (London, United Kingdom) in 2020.Application of 1072-53-3 This article mentions the following:
Post-translational modifications (PTMs) greatly expand the structures and functions of proteins in nature1,2. Although synthetic protein functionalization strategies allow mimicry of PTMs3,4, as well as formation of unnatural protein variants with diverse potential functions, including drug carrying5, tracking, imaging6 and partner crosslinking7, the range of functional groups that can be introduced remains limited. Here we describe the visible-light-driven installation of side chains at dehydroalanine residues in proteins through the formation of carbon-centered radicals that allow C-C bond formation in water. Control of the reaction redox allows site-selective modification with good conversions and reduced protein damage. In situ generation of boronic acid catechol ester derivatives generates RH2C· radicals that form the native (β-CH2-γ-CH2) linkage of natural residues and PTMs, whereas in situ potentiation of pyridylsulfonyl derivatives by Fe(II) generates RF2C· radicals that form equivalent β-CH2-γ-CF2 linkages bearing difluoromethylene labels. These reactions are chem. tolerant and incorporate a wide range of functionalities (more than 50 unique residues/side chains) into diverse protein scaffolds and sites. Initiation can be applied chemoselectively in the presence of sensitive groups in the radical precursors, enabling installation of previously incompatible side chains. The resulting protein function and reactivity are used to install radical precursors for homolytic on-protein radical generation; to study enzyme function with natural, unnatural and CF2-labeled post-translationally modified protein substrates via simultaneous sensing of both chemo- and stereoselectivity; and to create generalized ′alkylator proteins′ with a spectrum of heterolytic covalent-bond-forming activity (i.e., reacting diversely with small mols. at one extreme or selectively with protein targets through good mimicry at the other). Post-translational access to such reactions and chem. groups on proteins could be useful in both revealing and creating protein function. In the experiment, the researchers used many compounds, for example, 1,3,2-Dioxathiolane 2,2-dioxide (cas: 1072-53-3Application of 1072-53-3).
1,3,2-Dioxathiolane 2,2-dioxide (cas: 1072-53-3) belongs to benzothiophene derivatives. Benzothiophene is a fused ring compound of thiophene ring and benzene ring, which is an important class of heterocycles with advantageous structures. It is also used in the manufacturing of dyes such as thioindigo.Application of 1072-53-3
Referemce:
Benzothiophene – Wikipedia,
Benzothiophene | C8H6S – PubChem