ArticleACS central science2024
Peptide and Protein Cysteine Modification Enabled by Hydrosulfuration of Ynamide.
Article in ACS central science, 2024. 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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Who cites it
5 citing papers in PubMed.
- Article
- Achieving cysteine-selective peptide/protein bioconjugation via tunable triazine-pyridine chemistry.Science advances · 2025Article
- Electro-induced C-H/S-H cross-coupling for the functionalization/macrocyclization of cysteine-containing peptides.Nature communications · 2025Article
- Late-Stage Aromatic C-H Bond Functionalization for Cysteine/Selenocysteine Bioconjugation.Journal of the American Chemical Society · 2025Article
- Manganese-Catalyzed Electrochemical Diazidation of Dehydroalanine Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
Corrections and comments
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Efficient functionalization of peptides and proteins has widespread applications in chemical biology and drug discovery. However, the chemoselective and site-selective modification of proteins remains a daunting task. Herein, a highly efficient chemo-, regio-, and stereoselective hydrosulfuration of ynamide was identified as an efficient method for the precise modification of peptides and proteins by uniquely targeting the thiol group of cysteine (Cys) residues. This novel method could be facilely operated in aqueous buffer and was fully compatible with a wide range of proteins, including small model proteins and large full-length antibodies, without compromising their integrity and functions. Importantly, this reaction provides the
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Registered trials
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