ArticleJournal of the American Chemical Society2019
Genetically Introducing Biochemically Reactive Amino Acids Dehydroalanine and Dehydrobutyrine in Proteins.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 78 citations in OpenAlex.
- Advances in sulfonyl exchange chemical biology: expanding druggable target space.Chemical science · 2025Review
- Arginine Accelerates Sulfur Fluoride Exchange and Phosphorus Fluoride Exchange Reactions between Proteins.Angewandte Chemie (International ed. in English) · 2024Article
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Biospecific Chemistry for Covalent Linking of Biomacromolecules.Chemical reviews · 2024Review
- Article
- Genetically Encoded Epoxide Warhead for Precise and Versatile Covalent Targeting of Proteins.Journal of the American Chemical Society · 2024Article
- Fluorosulfate as a Latent Sulfate in Peptides and Proteins.Journal of the American Chemical Society · 2023Article
- The proximity-enabled sulfur fluoride exchange reaction in the protein context.Chemical science · 2023Article
- Residue selective crosslinking of proteins through photoactivatable or proximity-enabled reactivity.Current opinion in chemical biology · 2023Review
- Genetically encoded crosslinkers to address protein-protein interactions.Protein science : a publication of the Protein Society · 2023Review
- Sulfur(VI) fluorides as tools in biomolecular and medicinal chemistry.Organic & biomolecular chemistry · 2023Review
- Sulfur fluoride exchange.Nature reviews. Methods primers · 2023Article
- Late-Stage Modification of Oligopeptides by Nickel-Catalyzed Stereoselective Radical Addition to Dehydroalanine.Angewandte Chemie (International ed. in English) · 2022Article
- Relative Nuclease Resistance of a DNA Aptamer Covalently Conjugated to a Target Protein.International journal of molecular sciences · 2022Article
- New covalent bonding ability for proteins.Protein science : a publication of the Protein Society · 2022Review
- Methods for Studying Site-Specific O-GlcNAc Modifications: Successes, Limitations, and Important Future Goals.JACS Au · 2022Review
- Uncover New Reactivity of Genetically Encoded Alkyl Bromide Non-Canonical Amino Acids.Frontiers in chemistry · 2022Article
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- Writing and erasing O-GlcNAc from target proteins in cells.Biochemical Society transactions · 2021Article
- Halomethyl-Triazoles for Rapid, Site-Selective Protein Modification.Molecules (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Expansion of the genetic code with unnatural amino acids (Uaas) has significantly increased the chemical space available to proteins for exploitation. Due to the inherent limitation of translational machinery and the required compatibility with biological settings, function groups introduced via Uaas to date are restricted to chemically inert, bioorthogonal, or latent bioreactive groups. To break this barrier, here we report a new strategy enabling the specific incorporation of biochemically reactive amino acids into proteins. A latent bioreactive amino acid is genetically encoded at a position proximal to the target natural amino acid; they react via proximity-enabled reactivity, selectively converting the latter into a reactive residue in situ. Using this Genetically Encoded Chemical COnversion (GECCO) strategy and harnessing the sulfur-fluoride exchange (SuFEx) reaction between fluorosulfate-l-tyrosine and serine or threonine, we site-specifically generated the reactive dehydroalanine and dehydrobutyrine into proteins. GECCO works both inter- and intramolecularly, and is compatible with various proteins. We further labeled the resultant dehydroalanine-containing protein with thiol-saccharide to generate glycoprotein mimetics. GECCO represents a new solution for selectively introducing biochemically reactive amino acids into proteins and is expected to open new avenues for exploiting chemistry in live systems for biological research and engineering.
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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.