ArticleJournal of the American Chemical Society2025
Late-Stage Serine Modification Enables Noncanonical Peptide Synthesis.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
5 citing papers in PubMed.
- Site-Specific and Programmable Editing of Serine and Threonine in Unprotected Peptides.Journal of the American Chemical Society · 2026Article
- Benzodithiolane-Enabled C─O Bond Activation for Deoxygenative Functionalization of Carbohydrates and Nucleosides.Angewandte Chemie (International ed. in English) · 2026Article
- Photoredox-Catalyzed Lysine C(spJournal of the American Chemical Society · 2026Article
- Scaling SMILES-based chemical language models for therapeutic peptide engineering.bioRxiv : the preprint server for biology · 2026Article
- A Versatile Strategy for Head-to-Tail Macrocyclization and Traceless Backbone Editing of Short Peptides.Journal of the American Chemical Society · 2026Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Noncanonical amino acids play a critical role in enhancing drug efficacy, specificity, pharmacokinetics, and other key therapeutic properties. However, their incorporation into peptides or small molecules often presents significant synthetic challenges. Late-stage modification of natural residues, after the primary structural framework of a molecule is established, offers an efficient strategy for generating analogue libraries. Serine, one of the most abundant natural amino acids, remains underutilized due to the incompatibility of existing deoxygenative methods with complex peptides. Currently, no method is available for the late-stage modification of serine residues in peptides through carbon-carbon bond formation. Here, we address this gap by developing a site-selective, late-stage deoxygenative functionalization of serine residues. Inspired by automated DNA synthesis, we employ a phosphoramidite reagent in combination with a photocatalytic system to achieve efficient serine deoxygenative activation and radical addition to diverse acceptors, enabling the transformation of serine into various noncanonical residues such as homoglutamine, homoglutamic acid, 5-hydroxynorvaline, phosphonates, and alanine-3-
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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 Socratic graph.