Catalytic protein modification with dirhodium metallopeptides: specificity in designed and natural systems.
J Am Chem Soc
; 134(24): 10138-45, 2012 Jun 20.
Article
en En
| MEDLINE
| ID: mdl-22621321
ABSTRACT
In this study, we present advances in the use of rhodium(II) metallopeptides for protein modification. Site-specific, proximity-driven modification is enabled by the unique combination of peptide-based molecular recognition and a rhodium catalyst capable of modifying a wide range of amino-acid side chains. We explore catalysis based on coiled-coil recognition in detail, providing an understanding of the determinants of specificity and culminating in the demonstration of orthogonal modification of separate proteins in cell lysate. In addition, the concepts of proximity-driven catalysis are extended to include modification of the natural Fyn SH3 domain with metallopeptides based on a known proline-rich peptide ligand. The development of orthogonal catalyst-substrate pairs for modification in lysate, and the extension of these methods to new natural protein domains, highlight the capabilities for new reaction design possible in chemical approaches to site-specific protein modification.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Compuestos Organometálicos
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Péptidos
/
Rodio
/
Proteínas
Límite:
Humans
Idioma:
En
Revista:
J Am Chem Soc
Año:
2012
Tipo del documento:
Article
País de afiliación:
Estados Unidos