Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides.
Authors: Colombano, A., Dalponte, L., Dall'Angelo, S., Clemente, C., Idress, M., Ghazal, A. and Houssen, W.E.
Journal: Angew Chem Int Ed Engl
Volume: 62
Issue: 16
Pages: e202215979
eISSN: 1521-3773
DOI: 10.1002/anie.202215979
Abstract:Aromatic prenyltransferases from cyanobactin biosynthetic pathways catalyse the chemoselective and regioselective intramolecular transfer of prenyl/geranyl groups from isoprene donors to an electron-rich position in these macrocyclic and linear peptides. These enzymes often demonstrate relaxed substrate specificity and are considered useful biocatalysts for structural diversification of peptides. Herein, we assess the isoprene donor specificity of the N1-tryptophan prenyltransferase AcyF from the anacyclamide A8P pathway using a library of 22 synthetic alkyl pyrophosphate analogues, of which many display reactive groups that are amenable to additional functionalization. We further used AcyF to introduce a reactive moiety into a tryptophan-containing cyclic peptide and subsequently used click chemistry to fluorescently label the enzymatically modified peptide. This chemoenzymatic strategy allows late-stage modification of peptides and is useful for many applications.
https://eprints.bournemouth.ac.uk/38747/
Source: PubMed
Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides
Authors: Colombano, A., Dalponte, L., Dall'Angelo, S., Clemente, C., Idress, M., Ghazal, A. and Houssen, W.E.
Journal: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume: 62
Issue: 16
eISSN: 1521-3773
ISSN: 1433-7851
DOI: 10.1002/anie.202215979
https://eprints.bournemouth.ac.uk/38747/
Source: Web of Science (Lite)
Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides
Authors: Colombano, A., Houssen, W., Ghazal, A., Clemente, C., Idress, M., Dalponte, L. and Dall'Angelo, S.
Journal: Angewandte Chemie International Edition
Publisher: Wiley-Blackwell
eISSN: 1521-3773
ISSN: 1433-7851
DOI: 10.1002/anie.202215979
Abstract:Aromatic prenyltransferases from cyanobactin biosynthetic pathways catalyse the chemoselective and regioselective intramolecular transfer of prenyl/geranyl groups from isoprene donors to an electron-rich position in these macrocyclic and linear peptides. These enzymes often demonstrate relaxed substrate specificity and are considered useful biocatalysts for structural diversification of peptides. Herein, we assess the isoprene donor specificity of the N1-tryptophan prenyltransferase AcyF from the anacyclamide A8P pathway using a library of 22 synthetic alkyl pyrophosphate analogues, of which many display reactive groups that are amenable to additional functionalization. We further used AcyF to introduce a reactive moiety into a tryptophan-containing cyclic peptide and subsequently used click chemistry to fluorescently label the enzymatically modified peptide. This chemoenzymatic strategy allows late-stage modification of peptides and is useful for many applications.
https://eprints.bournemouth.ac.uk/38747/
Source: Manual
Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides.
Authors: Colombano, A., Dalponte, L., Dall'Angelo, S., Clemente, C., Idress, M., Ghazal, A. and Houssen, W.E.
Journal: Angewandte Chemie (International ed. in English)
Volume: 62
Issue: 16
Pages: e202215979
eISSN: 1521-3773
ISSN: 1433-7851
DOI: 10.1002/anie.202215979
Abstract:Aromatic prenyltransferases from cyanobactin biosynthetic pathways catalyse the chemoselective and regioselective intramolecular transfer of prenyl/geranyl groups from isoprene donors to an electron-rich position in these macrocyclic and linear peptides. These enzymes often demonstrate relaxed substrate specificity and are considered useful biocatalysts for structural diversification of peptides. Herein, we assess the isoprene donor specificity of the N1-tryptophan prenyltransferase AcyF from the anacyclamide A8P pathway using a library of 22 synthetic alkyl pyrophosphate analogues, of which many display reactive groups that are amenable to additional functionalization. We further used AcyF to introduce a reactive moiety into a tryptophan-containing cyclic peptide and subsequently used click chemistry to fluorescently label the enzymatically modified peptide. This chemoenzymatic strategy allows late-stage modification of peptides and is useful for many applications.
https://eprints.bournemouth.ac.uk/38747/
Source: Europe PubMed Central
Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides
Authors: Colombano, A., Dalponte, L., Dall'Angelo, S., Clemente, C., Idress, M., Ghazal, A. and Houssen, W.
Journal: Angewandte Chemie International Edition
Volume: 62
Issue: 16
Publisher: Wiley-Blackwell
ISSN: 1433-7851
Abstract:Aromatic prenyltransferases from cyanobactin biosynthetic pathways catalyse the chemoselective and regioselective intramolecular transfer of prenyl/geranyl groups from isoprene donors to an electron-rich position in these macrocyclic and linear peptides. These enzymes often demonstrate relaxed substrate specificity and are considered useful biocatalysts for structural diversification of peptides. Herein, we assess the isoprene donor specificity of the N1-tryptophan prenyltransferase AcyF from the anacyclamide A8P pathway using a library of 22 synthetic alkyl pyrophosphate analogues, of which many display reactive groups that are amenable to additional functionalization. We further used AcyF to introduce a reactive moiety into a tryptophan-containing cyclic peptide and subsequently used click chemistry to fluorescently label the enzymatically modified peptide. This chemoenzymatic strategy allows late-stage modification of peptides and is useful for many applications.
https://eprints.bournemouth.ac.uk/38747/
Source: BURO EPrints