Issue 4, 2011

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

Abstract

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 general strategy for protein modification on the basis of molecular shape. A broad range of peptideprotein interactions are potentially amenable to this approach.

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

Supplementary files

Article information

Article type
Edge Article
Submitted
09 Nov 2010
Accepted
07 Dec 2010
First published
21 Jan 2011

Chem. Sci., 2011,2, 690-695

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

B. V. Popp and Z. T. Ball, Chem. Sci., 2011, 2, 690 DOI: 10.1039/C0SC00564A

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