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Site-selective aqueous C-H acylation of tyrosine-containing oligopeptides with aldehydes.

ABSTRACT: The development of useful synthetic tools to label amino acids within a peptide framework for the ultimate modification of proteins in a late-stage fashion is a challenging task of utmost importance within chemical biology. Herein, we report the first Pd-catalyzed C-H acylation of a collection of Tyr-containing peptides with aldehydes. This water-compatible tagging technique is distinguished by its site-specificity, scalability and full tolerance of sensitive functional groups. Remarkably, it provides straightforward access to a high number of oligopeptides with altered side-chain topology including mimetics of endomorphin-2 and neuromedin N, thus illustrating its promising perspectives toward the diversification of structurally complex peptides and chemical ligation.

SUBMITTER: San Segundo M

PROVIDER: S-EPMC8162766 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Site-selective aqueous C-H acylation of tyrosine-containing oligopeptides with aldehydes.

San Segundo Marcos M Correa Arkaitz A

Chemical science 20201006 42

The development of useful synthetic tools to label amino acids within a peptide framework for the ultimate modification of proteins in a late-stage fashion is a challenging task of utmost importance within chemical biology. Herein, we report the first Pd-catalyzed C-H acylation of a collection of Tyr-containing peptides with aldehydes. This water-compatible tagging technique is distinguished by its site-specificity, scalability and full tolerance of sensitive functional groups. Remarkably, it pr ...[more]

PMID: 34094398

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