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Site-Selective Installation of Nϵ -Modified Sidechains into Peptide and Protein Scaffolds via Visible-Light-Mediated Desulfurative C-C Bond Formation.
Griffiths, Rhys C; Smith, Frances R; Long, Jed E; Scott, Daniel; Williams, Huw E L; Oldham, Neil J; Layfield, Robert; Mitchell, Nicholas J.
Affiliation
  • Griffiths RC; School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
  • Smith FR; School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
  • Long JE; Biodiscovery Institute, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
  • Scott D; School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, NG7 2UH, UK.
  • Williams HEL; Biodiscovery Institute, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
  • Oldham NJ; School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
  • Layfield R; School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, NG7 2UH, UK.
  • Mitchell NJ; School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
Angew Chem Int Ed Engl ; 61(2): e202110223, 2022 01 10.
Article in En | MEDLINE | ID: mdl-34713958
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 Nϵ -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 Nϵ Ac sidechain into recombinantly expressed ubiquitin (Ub).
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Proteins Language: En Journal: Angew Chem Int Ed Engl Year: 2022 Document type: Article Country of publication: Germany
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Proteins Language: En Journal: Angew Chem Int Ed Engl Year: 2022 Document type: Article Country of publication: Germany