ArticleNature communications2023
Suppression of alpha-carbon racemization in peptide synthesis based on a thiol-labile amino protecting group.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 25 citations in OpenAlex.
- Total Chemical Synthesis of Interleukin-15 and Interleukin-2: Taming Protein Hydrophobicity and Aggregation by a Versatile Solubilizing Strategy.Angewandte Chemie (International ed. in English) · 2026Article
- Solid-phase synthesis of sterically hindered peptides via ribosome-mimicking molecular reactors.Nature protocols · 2026Review
- Recent Advances in Metal-Based Catalysts for Nitrile Hydration to Amides: Mechanistic Aspects.Chemical record (New York, N.Y.) · 2026Review
- Aspartimide Formation and Its Prevention in Fmoc Chemistry Solid Phase Peptide Synthesis.Chembiochem : a European journal of chemical biology · 2025Review
- Fluorescent Antibiotics: Bridging Diagnostic and Therapy in the Fight against Bacterial Infections.Small science · 2025Review
- Chemical Synthesis of Human Proteoforms and Application in Biomedicine.ACS central science · 2024Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In conventional solid-phase peptide synthesis (SPPS), α-amino groups are protected with alkoxycarbonyl groups (e.g., 9-fluorenylmethoxycarbonyl [Fmoc]). However, during SPPS, inherent side reactions of the protected amino acids (e.g., α-C racemization and aspartimide formation) generate by-products that are hard to remove. Herein, we report a thiol-labile amino protecting group for SPPS, the 2,4-dinitro-6-phenyl-benzene sulfenyl (DNPBS) group, which is attached to the α-amino group via a S-N bond and can be quantitatively removed in minutes under nearly neutral conditions (1 M p-toluenethiol/pyridine). The use of DNPBS greatly suppresses the main side reactions observed during conventional SPPS. Although DNPBS SPPS is not as efficient as Fmoc SPPS, especially for synthesis of long peptides, DNPBS and Fmoc are orthogonal protecting groups; and thus DNPBS SPPS and Fmoc SPPS can be combined to synthesize peptides that are otherwise difficult to obtain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.