ArticleChemical science2020
Use of an asparaginyl endopeptidase for chemo-enzymatic peptide and protein labeling.
Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 65 citations in OpenAlex.
- Site-specific protein and peptide modification by redeploying an asparaginyl ligase for noncanonical reactions.Nature protocols · 2026Review
- "Lys-Leu" Motif Empowers ExpedientJACS Au · 2026Article
- Asparaginyl Ligases with Engineered Substrate Specificity for Controlled, Sequential Transpeptidation Reactions.Journal of the American Chemical Society · 2025Article
- Yeast as a tool for exploring disulfide-rich peptides.FEMS yeast research · 2025Review
- A Single Bioorthogonal Reaction for Multiplex Cell Surface Protein Labeling.Journal of the American Chemical Society · 2025Article
- An efficient and easily obtainable butelase variant for chemoenzymatic ligation and modification of peptides and proteins.Microbial cell factories · 2024Article
- Towards controlling activity of a peptide asparaginyl ligase (PAL) by lumazine synthetase compartmentalization.Faraday discussions · 2024Article
- Repurposing a plant peptide cyclase for targeted lysine acylation.Nature chemistry · 2024Article
- Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs.Communications chemistry · 2024Article
- Tertiary amide bond formation by an engineered asparaginyl ligase.Chemical science · 2024Article
- Intracellular Application of an Asparaginyl Endopeptidase for Producing Recombinant Head-to-Tail Cyclic Proteins.JACS Au · 2023Article
- C-terminal modification and functionalization of proteins via a self-cleavage tag triggered by a small molecule.Nature communications · 2023Article
- Recent advances and applications of peptide-agent conjugates for targeting tumor cells.Journal of cancer research and clinical oncology · 2023Review
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- On the design of a constitutively active peptide asparaginyl ligase for facile protein conjugation.FEBS open bio · 2023Article
- Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy.Bioconjugate chemistry · 2023Article
- OaAEP1 Ligase-Assisted Chemoenzymatic Synthesis of Full Cysteine-Rich Metal-Binding Cyanobacterial Metallothionein SmtA.Bioconjugate chemistry · 2023Article
- Engineered Nonviral Protein Cages Modified for MR Imaging.ACS applied bio materials · 2023Article
- Enzymatic Protein Immobilization on Amino-Functionalized Nanoparticles.Molecules (Basel, Switzerland) · 2023Article
- Combined Application of Orthogonal Sortases and Depsipeptide Substrates for Dual Protein Labeling.Bioconjugate chemistry · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Asparaginyl endopeptidases (AEPs) are ideal for peptide and protein labeling. However, because of the reaction reversibility, a large excess of labels or backbone modified substrates are needed. In turn, simple and cheap reagents can be used to label N-terminal cysteine, but its availability inherently limits the potential applications. Aiming to address these issues, we have created a chemo-enzymatic labeling system that exploits the substrate promiscuity of AEP with the facile chemical reaction between N-terminal cysteine and 2-formyl phenylboronic acid (FPBA). In this approach, AEP is used to ligate polypeptides with a Asn-Cys-Leu recognition sequence with counterparts possessing an N-terminal Gly-Leu. Instead of being a labeling reagent, the commercially available FPBA serves as a scavenger converting the byproduct Cys-Leu into an inert thiazolidine derivative. This consequently drives the AEP labeling reaction forward to product formation with a lower ratio of label to protein substrate. By carefully screening the reaction conditions for optimal compatibility and minimal hydrolysis, conversion to the ligated product in the model reaction resulted in excellent yields. The versatility of this AEP-ligation/FPBA-coupling system was further demonstrated by site-specifically labeling the N- or C-termini of various proteins.
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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.