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Synlett 2010(13): 1951-1954  
DOI: 10.1055/s-0030-1258132
LETTER
© Georg Thieme Verlag Stuttgart ˙ New York

Solid-Phase Synthesis of Phosphonylated Peptides

Mary MacDonald*, Marion Lanier, John Cashman
Human BioMolecular Research Institute, 5310 Eastgate Mall, San Diego, CA 92121, USA
Fax: +1(858)4589311; e-Mail: mmacdonald9@gmail.com;
Further Information

Publication History

Received 5 March 2010
Publication Date:
09 July 2010 (online)

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Abstract

We report the solid-phase syntheses of two series of phosphonylated peptides using Fmoc-protected amino acids. The peptides corresponded to regions containing phosphonylated Ser195 in the active site of butyrylcholinesterase and Tyr411 of ­human serum albumin. The phosphonylated Fmoc-protected amino acids were used in solid-phase peptide synthesis to prepare the peptides. Fmoc-serine and Fmoc-tyrosine with benzyl ester protection were treated with alkyl methylphosphonic monochloridates to phosphonylate the side-chain hydroxy groups. The phosphonylated peptides were designed to mimic the protein region after exposure of the proteins to organophosphorus agents.

Key words

organophosphonates - nerve agent - phosphonylated peptides - peptide synthesis - solid phase

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