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Langmuir. 2016 Jun 7;32(22):5480-90. doi: 10.1021/acs.langmuir.6b01020. Epub 2016 May 23.

Comparison of Zirconium Phosphonate-Modified Surfaces for Immobilizing Phosphopeptides and Phosphate-Tagged Proteins.

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Chimie et Interdisciplinarité: Synthèse Analyse Modélisation (CEISAM), Université de Nantes, CNRS, UMR 6230 , 2 rue de la Houssinière, BP 92208, 44322 Nantes Cedex 3, France.
Department of Chemistry, University of Florida , Gainesville, Florida 32611-7200, United States.
CRMD-CNRS, 1B rue de la férollerie, 45071 Orléans Cedex 2, France.
CNRS, CEMHTI UPR3079, Université de Orléans , F-45071 Orléans, France.
Fonctionnalité et Ingénierie des Protéines (UFIP), Université de Nantes, CNRS, UMR 6286 , 2 rue de la Houssinière BP 92208, 44322 Nantes Cedex 3, France.


Different routes for preparing zirconium phosphonate-modified surfaces for immobilizing biomolecular probes are compared. Two chemical-modification approaches were explored to form self-assembled monolayers on commercially available primary amine-functionalized slides, and the resulting surfaces were compared to well-characterized zirconium phosphonate monolayer-modified supports prepared using Langmuir-Blodgett methods. When using POCl3 as the amine phosphorylating agent followed by treatment with zirconyl chloride, the result was not a zirconium-phosphonate monolayer, as commonly assumed in the literature, but rather the process gives adsorbed zirconium oxide/hydroxide species and to a lower extent adsorbed zirconium phosphate and/or phosphonate. Reactions giving rise to these products were modeled in homogeneous-phase studies. Nevertheless, each of the three modified surfaces effectively immobilized phosphopeptides and phosphopeptide tags fused to an affinity protein. Unexpectedly, the zirconium oxide/hydroxide modified surface, formed by treating the amine-coated slides with POCl3/Zr(4+), afforded better immobilization of the peptides and proteins and efficient capture of their targets.

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