Article ID Journal Published Year Pages File Type
1164598 Analytica Chimica Acta 2013 6 Pages PDF
Abstract

•MIP for recognition of tyrosine phosphopeptides in aqueous media was prepared by epitope approach.•The MIPs demonstrated high adsorption capacity and selectivity for phenylphosphonic acid.•The MIP showed clear preference for tyrosine phosphopeptides over other peptides.

The tyrosine phosphorylation of proteins plays a vital role in signal transduction pathways. The highly selective enrichment of tyrosine phosphopeptides remains a significant challenge in this area of research because of the low levels of tyrosine phosphorylation in cells. Herein, we report the development of a novel molecularly imprinted polymer (MIP)-based method for the recognition of tyrosine phosphopeptides in aqueous media using an epitope approach. Phenylphosphonic acid, which has been regarded the “epitope” of phosphotyrosine, was used as a template, and commercially available zinc acrylate was used as a functional monomer to prepare the MIP. The one-pot synthetic process was simple, efficient, and the resulting MIPs were low-cost, robust, and recyclable. The MIP demonstrated significant higher levels of adsorption capacity and selectivity for phenylphosphonic acid than the non-imprinting polymer (NIP) over its structural analog benzoic acid. The MIP was also used as a molecular receptor to recognize tyrosine phosphopeptides in aqueous media, and showed a clear preference for tyrosine phosphopeptides over interfering serine peptides compared to TiO2. These results revealed the feasibility of the use of MIPs to effectively mimic the epitope approach, and provided a promising alternative to the immunoaffinity techniques commonly used for capturing tyrosine phosphopeptides.

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Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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