ArticleAngewandte Chemie (International ed. in English)2018
Post-Translational Backbone Engineering through Selenomethionine-Mediated Incorporation of Freidinger Lactams.
Article in Angewandte Chemie (International ed. in English), 2018. 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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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
8 citing papers in PubMed, 15 citations in OpenAlex.
- A selenoxide for single-atom protein modification of tyrosine residues enabled by water-resistant chalcogen and hydrogen bonding.Nature chemistry · 2025Article
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- Selenomethionine as an expressible handle for bioconjugations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Synthetic Elaboration of Native DNA by RASS (SENDR).ACS central science · 2020Article
- RASS-Enabled S/P-C and S-N Bond Formation for DEL Synthesis.Angewandte Chemie (International ed. in English) · 2020Article
- Expanding Reactivity in DNA-Encoded Library Synthesis via Reversible Binding of DNA to an Inert Quaternary Ammonium Support.Journal of the American Chemical Society · 2019Article
- Expanding the Scope of Protein Synthesis Using Modified Ribosomes.Journal of the American Chemical Society · 2019Article
- Novel protein science enabled by total chemical synthesis.Protein science : a publication of the Protein Society · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Amino-γ-lactam (Agl) bridged dipeptides, commonly known as Freidinger lactams, have been shown to constrain peptide backbone topology and stabilize type II' β-turns. The utility of these links as peptide constraints has inspired new approaches to their incorporation into complex peptides and peptoids, all of which require harsh reaction conditions or protecting groups that limit their use on unprotected peptides and proteins. Herein, we employ a mild and selective alkylation of selenomethionine in acidic aqueous solution, followed by immobilization of the alkylated peptide on to bulk reverse-phase C
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Registered trials
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