ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2016
Enzymatic Macrocyclization of 1,2,3-Triazole Peptide Mimetics.
Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed.
- 1,2,3-Triazoles as Biomimetics in Peptide Science.Molecules (Basel, Switzerland) · 2021Review
- Parallel lives of symbionts and hosts: chemical mutualism in marine animals.Natural product reports · 2018Review
- Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates.Nature communications · 2017Article
- Kinetic Landscape of a Peptide Bond-Forming Prolyl Oligopeptidase.Biochemistry · 2017Article
- Rapid protein immobilization for thin film continuous flow biocatalysis.Chemical communications (Cambridge, England) · 2016Article
- Enzymatic Macrocyclization of 1,2,3-Triazole Peptide Mimetics.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The macrocyclization of linear peptides is very often accompanied by significant improvements in their stability and biological activity. Many strategies are available for their chemical macrocyclization, however, enzyme-mediated methods remain of great interest in terms of synthetic utility. To date, known macrocyclization enzymes have been shown to be active on both peptide and protein substrates. Here we show that the macrocyclization enzyme of the cyanobactin family, PatGmac, is capable of macrocyclizing substrates with one, two, or three 1,4-substituted 1,2,3-triazole moieties. The introduction of non-peptidic scaffolds into macrocycles is highly desirable in tuning the activity and physical properties of peptidic macrocycles. We have isolated and fully characterized nine non-natural triazole-containing cyclic peptides, a further ten molecules are also synthesized. PatGmac has now been shown to be an effective and versatile tool for the ring closure by peptide bond formation.
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Registered trials
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