Metal-Catalyzed C(sp2)−H Functionalization Processes of Phenylalanine- and Tyrosine-Containing Peptides
The site-selective chemical diversification of biomolecules constitutes an unmet challenge of capital importance within medicinal chemistry and chemical biology. The functionalization of otherwise unreactive C-H bonds holds great promise for reducing the reliance on existing functional groups, there...
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2021 |
| País: | España |
| Institución: | Universidad del País Vasco |
| Repositorio: | Addi. Archivo Digital para la Docencia y la Investigación |
| OAI Identifier: | oai:addi.ehu.eus:10810/55017 |
| Acceso en línea: | http://hdl.handle.net/10810/55017 |
| Access Level: | acceso abierto |
| Palabra clave: | C-H functionalization homogeneous catalysis late-stage modification peptides phenylalanine tyrosine C-H activation alpha-amino-acid unactivated C(SP(3))-H bonds PD(II)-catalyzed amination single-electron side-chains derivatives macrocyclization picolinamide olefination |
| Sumario: | The site-selective chemical diversification of biomolecules constitutes an unmet challenge of capital importance within medicinal chemistry and chemical biology. The functionalization of otherwise unreactive C-H bonds holds great promise for reducing the reliance on existing functional groups, thereby streamlining chemical syntheses. Over the last years, a myriad of peptide labelling techniques featuring metal-catalyzed C-H functionalization reactions have been developed. Despite the wealth of reports in the field, the site-selective modification of both phenylalanine (Phe) and tyrosine (Tyr) compounds upon metal catalysis remain comparatively overlooked. This review highlights these promising tagging strategies, which generally occur through the formation of challenging 6-membered metallacycles and enable the late-stage diversification of peptides in a tailored fashion. |
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