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Issue 20, 2012
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Triazole phosphohistidine analogues compatible with the Fmoc-strategy

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Abstract

Phosphorylation of histidine is essential for bacterial two-component signalling; its importance to modulation of eukaryotic protein function remains undefined. Until recently, no immunochemical probes of this post-translational modification existed, however triazole phosphonate analogues of this modified amino acid have now been applied to the generation of site-specific antibodies. The protecting group strategy used in the original report is incompatible with standard protocols for Fmoc-solid phase peptide synthesis. In this paper, we report the application of P(III) chemistry to generate the complementary dibenzyl and di-tert-butyl phosphonate esters. These forms of the triazole analogue are fully compatible with standard Fmoc-SPPS and are therefore ideal for wider application by the chemical and biochemical community.

Graphical abstract: Triazole phosphohistidine analogues compatible with the Fmoc-strategy

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Publication details

The article was received on 19 Dec 2011, accepted on 19 Mar 2012 and first published on 20 Mar 2012


Article type: Paper
DOI: 10.1039/C2OB25517K
Citation: Org. Biomol. Chem., 2012,10, 4043-4049
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    Triazole phosphohistidine analogues compatible with the Fmoc-strategy

    T. E. M<small xmlns="http://www.rsc.org/schema/rscart38"> <sup>c</sup> </small>Allister and M. E. Webb, Org. Biomol. Chem., 2012, 10, 4043
    DOI: 10.1039/C2OB25517K

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