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Issue 4, 2011
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Proximity-driven metallopeptide catalysis: Remarkable side-chain scope enables modification of the Fos bZip domain

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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

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Publication details

The article was received on 09 Nov 2010, accepted on 07 Dec 2010 and first published on 21 Jan 2011


Article type: Edge Article
DOI: 10.1039/C0SC00564A
Citation: Chem. Sci., 2011,2, 690-695
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    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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