ArticleJournal of the American Chemical Society2022
Generation of Proteins with Free N-Terminal Cysteine by Aminopeptidases.
Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- "Lys-Leu" Motif Empowers ExpedientJACS Au · 2026Article
- Combinatorial mutagenesis of N-terminal sequences reveals unexpected and expanded stability determinants of thebioRxiv : the preprint server for biology · 2025Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Tunable Heteroaromatic Nitriles for Selective Bioorthogonal Click Reaction with Cysteine.Bioconjugate chemistry · 2023Article
- Catalyst-free thiazolidine formation chemistry enables the facile construction of peptide/protein-cell conjugates (PCCs) at physiological pH.Chemical science · 2023Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Efficient, site-specific, and bio-orthogonal conjugation of chemical functionalities to proteins is of great utility in fundamental research as well as industrial processes (e.g., the production of antibody-drug conjugates and immobilization of enzymes for biocatalysis). A popular approach involves reacting a free N-terminal cysteine with a variety of electrophilic reagents. However, current methods for generating proteins with N-terminal cysteines have significant limitations. Herein we report a novel, efficient, and convenient method for producing recombinant proteins with free N-terminal cysteines by genetically fusing a Met-Pro-Cys sequence to the N-terminus of a protein of interest and subjecting the recombinant protein to the sequential action of methionine and proline aminopeptidases. The resulting protein was site-specifically labeled at the N-terminus with fluorescein and a cyclic cell-penetrating peptide through native chemical ligation and a 2-cyanobenzothiazole moiety, respectively. In addition, the optimal recognition sequence of
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