ArticleBiomolecules2022
Halogenation of Peptides and Proteins Using Engineered Tryptophan Halogenase Enzymes.
Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Enzymatic Bromination of Native Peptides for Late-Stage Structural Diversification via Suzuki-Miyaura Coupling.ACS chemical biology · 2026Article
- From marine predator to pharmacology: Conotoxin diversity, discovery, and therapeutic potential.Zoological research · 2026Review
- Enzymatic bromination of native peptides for late-stage structural diversification via Suzuki-Miyaura coupling.bioRxiv : the preprint server for biology · 2025Article
- Peptidic Tryptophan Halogenation by a Promiscuous Flavin-Dependent Enzyme.Angewandte Chemie (International ed. in English) · 2025Article
- Structural Basis of Regioselective Bromination of Tricyclic Tryptoline by the Tryptophan Halogenase Thal.Chembiochem : a European journal of chemical biology · 2025Article
- Recent Advances in Augmenting the Therapeutic Efficacy of Peptide-Drug Conjugates.Journal of medicinal chemistry · 2025Review
- Biosynthesis of Halogenated Tryptophans for Protein Engineering Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Recent advances in the development of therapeutic peptides.Trends in pharmacological sciences · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Halogenation of bioactive peptides via incorporation of non-natural amino acid derivatives during chemical synthesis is a common strategy to enhance functionality. Bacterial tyrptophan halogenases efficiently catalyze regiospecific halogenation of the free amino acid tryptophan, both in vitro and in vivo. Expansion of their substrate scope to peptides and proteins would facilitate highly-regulated post-synthesis/expression halogenation. Here, we demonstrate novel in vitro halogenation (chlorination and bromination) of peptides by select halogenase enzymes and identify the C-terminal (G/S)GW motif as a preferred substrate. In a first proof-of-principle experiment, we also demonstrate chemo-catalyzed derivatization of an enzymatically chlorinated peptide, albeit with low efficiency. We further rationally derive PyrH halogenase mutants showing improved halogenation of the (G/S)GW motif, both as a free peptide and when genetically fused to model proteins with efficiencies up to 90%.
Indexed as
Identifiers
What OpenQuestion holds
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.