1516-27-4Relevant articles and documents
Synthetic approach for unsaturated precursors for parahydrogen induced polarization of choline and its analogs
Shchepin, Roman V.,Chekmenev, Eduard Y.
, p. 655 - 662 (2013)
Reported here are (i) a new synthetic approach for preparation of (ii) a new compound class, of -OH, for example, an -OH group is replaced with acetyl protecting group, protected 1,2-dehydrocholine analogs and (iii) a new synthetic route for betaine aldehyde. The C=C bond of 1,2-dehydrocholine moiety can be used for molecular addition of parahydrogen producing -OH protected hyperpolarized choline by parahydrogen-induced polarization (PHIP). The reported synthetic approach allows for incorporation of 15N and deuterium labels, which are necessary for preparation of highly polarized PHIP contrast agents. Isotope labeling with 15N and/or deuterium was conducted. Hyperpolarized 15N-choline enabled by the reported synthetic approach can be potentially used as an imaging biomarker of cancer similar to choline positron emission tomography tracers. Copyright
Site-Selective Installation of N?-Modified Sidechains into Peptide and Protein Scaffolds via Visible-Light-Mediated Desulfurative C–C Bond Formation
Griffiths, Rhys C.,Layfield, Robert,Long, Jed E.,Mitchell, Nicholas J.,Oldham, Neil J.,Scott, Daniel,Smith, Frances R.,Williams, Huw E. L.
supporting information, (2021/12/08)
Post-translational modifications (PTMs) enhance the repertoire of protein function and mediate or influence the activity of many cellular processes. The preparation of site-specifically and homogeneously modified proteins, to apply as tools to understand the biological role of PTMs, is a challenging task. Herein, we describe a visible-light-mediated desulfurative C(sp3)–C(sp3) bond forming reaction that enables the site-selective installation of N?-modified sidechains into peptides and proteins of interest. Rapid, operationally simple, and tolerant to ambient atmosphere, we demonstrate the installation of a range of lysine (Lys) PTMs into model peptide systems and showcase the potential of this technology by site-selectively installing an N?Ac sidechain into recombinantly expressed ubiquitin (Ub).