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Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
Published on: January 11, 2017
Fmoc-chemistry of a stable phosphohistidine analogue
Tom E McAllister1, Michael G Nix, Michael E Webb
1School of Chemistry, University of Leeds, Leeds, UK.
Abstract:
We report the synthesis of the phosphohistidine analogue, Fmoc-4-diethylphosphonotriazolylalanine 5 and its incorporation into peptides. Our synthesis of 5 has enabled us to demonstrate that the analogue is compatible with Fmoc-solid phase peptide synthesis (SPPS) conditions. Standard cleavage conditions yield the diethyl phosphonate-protected peptide, however this can be subsequently deprotected using trimethylsilyl bromide to yield the free phosphonic acid-containing peptides.

