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The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy
Peptides play many key roles in biological systems and numerous methods have been developed to generate both natural and unnatural peptides. However, straightforward, reliable coupling methods that can be achieved under mild reactions conditions are still sought after. In this work, a new N-terminal...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
RSC
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9906322/ https://www.ncbi.nlm.nih.gov/pubmed/36794017 http://dx.doi.org/10.1039/d2cb00237j |
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author | Ni, Yeke Wang, Yu Tabor, Alethea B. Ward, John M. Hailes, Helen C. |
author_facet | Ni, Yeke Wang, Yu Tabor, Alethea B. Ward, John M. Hailes, Helen C. |
author_sort | Ni, Yeke |
collection | PubMed |
description | Peptides play many key roles in biological systems and numerous methods have been developed to generate both natural and unnatural peptides. However, straightforward, reliable coupling methods that can be achieved under mild reactions conditions are still sought after. In this work, a new N-terminal tyrosine-containing peptide ligation method with aldehydes, utilising a Pictet–Spengler reaction is described. In a key step, tyrosinase enzymes have been used to convert l-tyrosine to l-3,4-dihydroxyphenyl alanine (l-DOPA) residues, generating suitable functionality for the Pictet–Spengler coupling. This new chemoenzymatic coupling strategy can be used for fluorescent-tagging and peptide ligation purposes. |
format | Online Article Text |
id | pubmed-9906322 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | RSC |
record_format | MEDLINE/PubMed |
spelling | pubmed-99063222023-02-14 The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy Ni, Yeke Wang, Yu Tabor, Alethea B. Ward, John M. Hailes, Helen C. RSC Chem Biol Chemistry Peptides play many key roles in biological systems and numerous methods have been developed to generate both natural and unnatural peptides. However, straightforward, reliable coupling methods that can be achieved under mild reactions conditions are still sought after. In this work, a new N-terminal tyrosine-containing peptide ligation method with aldehydes, utilising a Pictet–Spengler reaction is described. In a key step, tyrosinase enzymes have been used to convert l-tyrosine to l-3,4-dihydroxyphenyl alanine (l-DOPA) residues, generating suitable functionality for the Pictet–Spengler coupling. This new chemoenzymatic coupling strategy can be used for fluorescent-tagging and peptide ligation purposes. RSC 2022-12-12 /pmc/articles/PMC9906322/ /pubmed/36794017 http://dx.doi.org/10.1039/d2cb00237j Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Ni, Yeke Wang, Yu Tabor, Alethea B. Ward, John M. Hailes, Helen C. The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy |
title | The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy |
title_full | The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy |
title_fullStr | The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy |
title_full_unstemmed | The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy |
title_short | The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy |
title_sort | use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9906322/ https://www.ncbi.nlm.nih.gov/pubmed/36794017 http://dx.doi.org/10.1039/d2cb00237j |
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