Peptide macrocyclisation intramolecular interception of visible-light-mediated desulfurisation
Synthetic methods that enable the macrocyclisation of peptides facilitate the development of effective therapeutic and diagnostic tools. Herein we report a peptide cyclisation strategy based on intramolecular interception of visible-light-mediated cysteine desulfurisation. This method allows cyclisa...
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| Veröffentlicht in: | Chemical science (Cambridge) 2024-06, Vol.15 (25), p.9612-9619 |
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| container_title | Chemical science (Cambridge) |
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| creator | Smith, Frances R Meehan, Declan Griffiths, Rhys C Knowles, Harriet J Zhang, Peiyu Williams, Huw E. L Wilson, Andrew J Mitchell, Nicholas J |
| description | Synthetic methods that enable the macrocyclisation of peptides facilitate the development of effective therapeutic and diagnostic tools. Herein we report a peptide cyclisation strategy based on intramolecular interception of visible-light-mediated cysteine desulfurisation. This method allows cyclisation of unprotected peptides in an aqueous solution
via
the installation of a hydrocarbon linkage. We explore the limits of this chemistry using a range of model peptides of increasing length and complexity, including peptides of biological/therapeutic relevance. The method is applied to replace the native disulfide of the peptide hormone, oxytocin, with a proteolytically/redox-stable hydrocarbon, and internal macrocyclisation of an MCL-1-binding peptide.
Herein, we report a peptide cyclisation strategy
via
intramolecular interception of cysteine desulfurisation. This method enables the cyclisation of unprotected peptides in aqueous solution
via
the installation of a hydrocarbon linkage. |
| doi_str_mv | 10.1039/d3sc05865d |
| format | Article |
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via
the installation of a hydrocarbon linkage. We explore the limits of this chemistry using a range of model peptides of increasing length and complexity, including peptides of biological/therapeutic relevance. The method is applied to replace the native disulfide of the peptide hormone, oxytocin, with a proteolytically/redox-stable hydrocarbon, and internal macrocyclisation of an MCL-1-binding peptide.
Herein, we report a peptide cyclisation strategy
via
intramolecular interception of cysteine desulfurisation. This method enables the cyclisation of unprotected peptides in aqueous solution
via
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via
the installation of a hydrocarbon linkage. We explore the limits of this chemistry using a range of model peptides of increasing length and complexity, including peptides of biological/therapeutic relevance. The method is applied to replace the native disulfide of the peptide hormone, oxytocin, with a proteolytically/redox-stable hydrocarbon, and internal macrocyclisation of an MCL-1-binding peptide.
Herein, we report a peptide cyclisation strategy
via
intramolecular interception of cysteine desulfurisation. This method enables the cyclisation of unprotected peptides in aqueous solution
via
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via
the installation of a hydrocarbon linkage. We explore the limits of this chemistry using a range of model peptides of increasing length and complexity, including peptides of biological/therapeutic relevance. The method is applied to replace the native disulfide of the peptide hormone, oxytocin, with a proteolytically/redox-stable hydrocarbon, and internal macrocyclisation of an MCL-1-binding peptide.
Herein, we report a peptide cyclisation strategy
via
intramolecular interception of cysteine desulfurisation. This method enables the cyclisation of unprotected peptides in aqueous solution
via
the installation of a hydrocarbon linkage.</abstract><doi>10.1039/d3sc05865d</doi><tpages>8</tpages></addata></record> |
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| title | Peptide macrocyclisation intramolecular interception of visible-light-mediated desulfurisation |
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