ArticleAngewandte Chemie (International ed. in English)2020
Efficient Chemical Protein Synthesis using Fmoc-Masked N-Terminal Cysteine in Peptide Thioester Segments.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- 4-Formyl-N-Methylpyridinium-Mediated N-Terminal Cysteine Modification/Removal Facilitates One-Pot Multiplex Peptide Ligation.Angewandte Chemie (International ed. in English) · 2026Article
- An efficient method for site-selective boronation of peptides and proteins applied in magnified bacterial imaging.Nature communications · 2025Article
- An Elegant Method of One-Pot Ligation-Desulfurization for High-Yielding Chemical Protein Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Chemical Protein Engineering: Backbone Cyclization Rescues Folding of a 183-Residue Truncated Domain of Malaria Parasite Protein PfAMA1.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Total Chemical Synthesis of a Functionalized GFP Nanobody.Chembiochem : a European journal of chemical biology · 2022Article
- Redox-Controlled Chemical Protein Synthesis: Sundry Shades of Latency.Accounts of chemical research · 2022Article
- One-Pot Chemical Protein Synthesis Utilizing Fmoc-Masked Selenazolidine to Address the Redox Functionality of Human Selenoprotein F.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Efficient Chemical Protein Synthesis using Fmoc-Masked N-Terminal Cysteine in Peptide Thioester Segments.Angewandte Chemie (International ed. in English) · 2020Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
We report an operationally simple method to facilitate chemical protein synthesis by fully convergent and one-pot native chemical ligations utilizing the fluorenylmethyloxycarbonyl (Fmoc) moiety as an N-masking group of the N-terminal cysteine of the middle peptide thioester segment(s). The Fmoc group is stable to the harsh oxidative conditions frequently used to generate peptide thioesters from peptide hydrazide or o-aminoanilide. The ready availability of Fmoc-Cys(Trt)-OH, which is routinely used in Fmoc solid-phase peptide synthesis, where the Fmoc group is pre-installed on cysteine residue, minimizes additional steps required for the temporary protection of the N-terminal cysteinyl peptides. The Fmoc group is readily removed after ligation by short exposure (<7 min) to 20 % piperidine at pH 11 in aqueous conditions at room temperature. Subsequent native chemical ligation reactions can be performed in presence of piperidine in the same solution at pH 7.
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