Proximity-driven metallopeptide catalysis: Remarkable side-chain scope enables modification of the Fos bZip domain

Coiled-coil assembly of substrate peptides with dirhodium metallopeptide catalysts enables side-chain modification on the basis of molecular shape. A wide range of amino acids are effectively modified, including the first examples of carboxamide (glutamine and asparagine) modification. The method is...

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Bibliographic Details
Published in:Chemical science (Cambridge) 2011-01, Vol.2 (4), p.690-695
Main Authors: Popp, Brian V., Ball, Zachary T.
Format: Article
Language:English
Subjects:
Amino acids
Assembly
Catalysis
Catalysts
Coiling
Covalence
Residues
Strategy
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Summary:Coiled-coil assembly of substrate peptides with dirhodium metallopeptide catalysts enables side-chain modification on the basis of molecular shape. A wide range of amino acids are effectively modified, including the first examples of carboxamide (glutamine and asparagine) modification. The method is used to achieve covalent modification of the c-Fos bZip domain at different residues, depending on the metallopeptide structure. By combining promiscuous catalytic reactivity with specific molecular recognition, this work establishes a genera] strategy for protein modification on the basis of molecular shape. A broad range of peptide-protein interactions are potentially amenable to this approach.
ISSN:2041-6520
2041-6539
DOI:10.1039/c0sc00564a