Late-Stage Diversification of Tryptophan-Derived Biomolecules |
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Authors: | Hendrik Gruß Prof. Dr. Norbert Sewald |
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Affiliation: | Organische und Bioorganische Chemie, Fakultät für Chemie, Universität Bielefeld, Universitätsstraße 25, 33615 Bielefeld, Germany |
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Abstract: | Pd-mediated reactions have emerged as a powerful tool for the site-selective and bioorthogonal late-stage diversification of amino acids, peptides and related compounds. Indole moieties of tryptophan derivatives are susceptible to C2H-activation, whereas halogenated aromatic amino acids such as halophenylalanines or halotryptophans provide a broad spectrum of different functionalisations. The compatibility of transition-metal-catalysed cross-couplings with functional groups in peptides, other biologically active compounds and even proteins has been demonstrated. This Review primarily compiles the application of different cross-coupling reactions to modify halotryptophans, halotryptophan containing peptides or halogenated, biologically active compounds derived from tryptophan. Modern approaches use regio- and stereoselective biocatalytic strategies to generate halotryptophans and derivatives on a preparative scale. The combination of bio- and chemocatalysis in cascade reactions is given by the biocompatibility and bioorthogonality of Pd-mediated reactions. |
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Keywords: | cross-coupling enzymatic halogenation late-stage diversification palladium catalysis tryptophans |
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