ArticleChemistryOpen2018
Utility of the Phenacyl Protecting Group in Traceless Protein Semisynthesis through Ligation-Desulfurization Chemistry.
Article in ChemistryOpen, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- HSP27 Inhibitory Activity against Caspase-3 Cleavage and Activation by Caspase-9 Is Enhanced by Chaperone O-GlcNAc ModificationACS chemical biology · 2023Article
- OaAEP1 Ligase-Assisted Chemoenzymatic Synthesis of Full Cysteine-Rich Metal-Binding Cyanobacterial Metallothionein SmtA.Bioconjugate chemistry · 2023Article
- On-Demand Detachment of Succinimides on Cysteine to Facilitate (Semi)Synthesis of Challenging Proteins.Journal of the American Chemical Society · 2020Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019Review
- Utility of the Phenacyl Protecting Group in Traceless Protein Semisynthesis through Ligation-Desulfurization Chemistry.ChemistryOpen · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Semisynthesis of proteins via expressed protein ligation is a widely applicable method, even more so because of the possibility of ligation at non-cysteine sites using β-mercapto amino acids that can be converted to the corresponding native amino acids by desulfurization. A drawback of this ligation- desulfurization approach is the removal of any unprotected native cysteine residues within the ligated protein segments. Here, we show that the phenacyl (PAc) moiety can be successfully used to protect cysteines within recombinantly generated protein segments. As such, this group was selectively appended onto cysteine side chains within bacterially expressed polypeptides following intein cleavage, which reveals a rather sensitive thioester at the C-terminus. The PAc group proved to be compatible with native chemical ligation, radical desulfurization, and reverse-phase HPLC conditions, and was smoothly removed at the end. The utility of the PAc protecting group was then demonstrated by the 'traceless' semisynthesis of two proteins containing one or two native cysteines: human small heat shock protein Hsp27 and murine prion protein.
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