title: Triazole phosphohistidine analogues compatible with the Fmoc-strategy.
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.
authors.affiliation: Astbury Centre for Structural Molecular Biology and School of Chemistry, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK.
authors.forename: Tom E
authors.initials: TE
authors.lastname: McAllister
authors.forename: Michael E
authors.initials: ME
authors.lastname: Webb
mesh_terms: D006639:Histidine / Q000031:analogs & derivatives* / Q000737:chemistry; D007536:Isomerism; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry; D014230:Triazoles / Q000737:chemistry*
chemical_list: D010455:Peptides; D014230:Triazoles; D006639:Histidine; C005436:phosphohistidine