One-pot synthesis of phenylphosphonic acid imprinted polymers for tyrosine phosphopeptides recognition in aqueous phase

Li, Quishui; Shen, Feng; Zhang, Xiao; Hu, Yu‐Feng; Zhang, Qingxi; Xu, Lin; Ren, Xueqin

doi:10.1016/j.aca.2013.07.040

Cited by 47 publications

(37 citation statements)

References 28 publications

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“…Additionally, the need to retain the template in the same conformational state as that found for the native state of the biomacromolecule may not have to be as stringently controlled, since the biomacromolecular target molecule is not involved in the MIP preparation and only needs to bind to the imprinted cavity with sufficient affinity as dictated by the application requirements. A summary of monoliths [62][63][64][65] and particles/beads [59,60,[66][67][68][69][70][71][72][73][74] made using the epitope approach is shown in Tables 1 and 2, respectively.…”

Section: Epitope/protein Substructure Imprintingmentioning

confidence: 99%

Advances in the development of molecularly imprinted polymers for the separation and analysis of proteins with liquid chromatography

Boysen

2018

J of Separation Science

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This review documents recent advances in the design, synthesis, characterization, and application of molecularly imprinted polymers in the form of monoliths and particles/beads for the use in the separation and analysis of proteins with solid‐phase extraction or liquid chromatography. The merits of three‐dimensional molecular imprinting, whereby the molecular template is randomly embedded in the polymer, and two‐dimensional imprinting, in which the template is confined to the surface, are described. Target protein binding can be achieved by either using the entire protein as a template or by using a protein substructure as template, that is, a peptide, as in the "epitope" approach. The intended approach and strategy then determine the choice of polymerization method. A synopsis has been provided on methods used for the physical, chemical, and functional characterizations and associated performance evaluations of molecularly imprinted and nonimprinted control polymers, involving a diverse range of analytical techniques commonly used for low and high molecular mass analytes. Examples of recent applications demonstrate that, due to the versatility of imprinting methods, molecularly imprinted monoliths or particles/beads can be adapted to protein extraction/depletion and separation procedures relevant to, for example, protein biomarker detection and quantification in biomedical diagnostics and targeted proteomics.

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Section: Epitope/protein Substructure Imprintingmentioning

confidence: 99%

Advances in the development of molecularly imprinted polymers for the separation and analysis of proteins with liquid chromatography

Boysen

2018

J of Separation Science

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“…In 2013, Ren and co‐workers prepared a highly specific MIP by polymerizing zinc acrylate and using phenylphosphonic acid as the template: this could be regarded as the “epitope” of phosphotyrosine ( Figure a). This MIP exhibited a strong adsorption capacity for tyrosine PPs (e.g., TRG[pY]GTSTRL), which was two times higher than that for serine or threonine PPs (e.g., TVDME[pS]TEVF and GP[pT]LTYGAR).…”

Section: Polymeric Materials For Phosphorylated Peptide (Pp) Enrichmentmentioning

confidence: 99%

“…a) Typical preparation process of a molecularly imprinted polymer (MIP) for specific recognition and capture of phosphorylated tyrosine (pTyr) peptide . b) Temperature‐modulated adsorption and desorption process of phosphopeptides (PPs) on a smart polymer surface.…”

Section: Polymeric Materials For Phosphorylated Peptide (Pp) Enrichmentmentioning

confidence: 99%

New Opportunities and Challenges of Smart Polymers in Post‐Translational Modification Proteomics

et al. 2017

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Protein post-translational modifications (PTMs), which denote covalent additions of various functional groups (e.g., phosphate, glycan, methyl, or ubiquitin) to proteins, significantly increase protein complexity and diversity. PTMs play crucial roles in the regulation of protein functions and numerous cellular processes. However, in a living organism, native PTM proteins are typically present at substoichiometric levels, considerably impeding mass-spectrometry-based analyses and identification. Over the past decade, the demand for in-depth PTM proteomics studies has spawned a variety of selective affinity materials capable of capturing trace amounts of PTM peptides from highly complex biosamples. However, novel design ideas or strategies are urgently required for fulfilling the increasingly complex and accurate requirements of PTM proteomics analysis, which can hardly be met by using conventional enrichment materials. Considering two typical types of protein PTMs, phosphorylation and glycosylation, an overview of polymeric enrichment materials is provided here, with an emphasis on the superiority of smart-polymer-based materials that can function in intelligent modes. Moreover, some smart separation materials are introduced to demonstrate the enticing prospects and the challenges of smart polymers applied in PTM proteomics.

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“…[125][126][127][128][129][130][131][132][133] The first attempt to apply molecular imprinting technology for phosphoproteomics was reported by Sellergren et al 125 The neutral urea-based receptor was synthesized using N, C-protected phosphotyrosine as a template and ethylene glycol dimethacrylate (EDMA) as a crosslinker. This crushed monolith material 26 …”

Section: Mips For Phosphoproteomicsmentioning

confidence: 99%

“…In another approach, the monodisperse 4-vinylpyridine-based MIPs targeting organophosphates were shown to non-selectively trap phosphorylated peptides (pSer, pThr, pTyr) and phosphopeptides from a tryptic digest of α-casein. 126 Ren et al 127,128 have used charged metal ion-based functional monomers (Zn 2+ and Ti 4+ ) for imprinting of phenylphosphonic acid (PPA) as an epitope template. Obtained materials displayed the affinity for phosphorylated peptides in aqueous solution with a preference for tyrosine phosphorylated peptides as contrasted with unbiased enrichment with TiO 2 .…”

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confidence: 99%

New fractionation tools targeting elusive post-translational modifications

Wierzbicka¹

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Protein phosphorylation is a reversible post-translational modification (PTM) playing a central role in numerous biological events including disease pathogenesis. Thus, the analysis of phosphoproteome is crucial for understanding cellular regulation processes and can facilitate the development of new diagnostic and therapeutic tools. Phosphoproteins are typically analyzed using liquid chromatography coupled with mass spectrometry (LC-MS) after proteolytic processing. However, phosphopeptides are notoriously difficult to analyze by LC-MS due their low abundance and transient nature. This creates a need for effective enrichment tools for phosphorylated proteins and peptides prior to mass spectrometry analysis.The work presented in this thesis is focused on development and validation of methods and tools for enrichment of phosphopeptides with the use of molecular imprinting technology. In particular, the targeted PTMs include phosphorylation on tyrosine (pTyr) and histidine (pHis).The key recognition element employed in developed synthetic receptors was 1,3-diaryl urea functional monomer FM1. This monomer is a potent hydrogen bond donor forming strong cyclic hydrogen bonds with oxyanions such as phosphates. The bias of the imprinted urea-based receptor towards different phosphorylated residues can be programmed by selection of the template. Thus, the N, C-protected phosphotyrosine and phosphonotriazolylalanine were used as templates to generate phosphotyrosine (pTyr MIP) and phosphohistidine (pHis MIP) selective molecularly imprinted polymers, respectively.The application of previously reported pTyr MIP for phosphoproteomic studies was validated on complex biological samples of the mouse brain lysate digest spiked with standard peptides and HeLa cells digested proteins. Furthermore, the pTyr MIP was developed in the format of microspherical porous 9 beads characterized by uniformly sized and shaped particles with increased surface area and pore size as well as improved binding affinity and selectivity for larger pTyr peptides (2-3 kDa). This opens the way to generation of capture materials suitable for middle-down phosphoproteomics.In response to the lack of adequate tools and methods for enrichment of acid-labile phosphohistidine peptides a pHis MIP-based approach is proposed as a solution. The method involving selective dephosphorylation of phosphoserine (pSer) peptide by alkali treatment of the sample, followed by extraction of base-stable pHis peptides with MIP was demonstrated on the sample of bovine serum albumin digest spiked with standard pSer and pHis peptides.The last part of this thesis is focused on improving the recognition of phosphopeptides in aqueous media -the natural environment of biological samples. Guided by the principles of supramolecular chemistry, novel cationic host monomers were introduced for binding phosphates by ionic hydrogen bonds. These were used to synthesize MIPs showing enhanced binding of phosphopeptides in aqueous media. 10 11 POPULÄRVETENSKAPLIG SAMMANFATTNINGMänniskok...

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One-pot synthesis of phenylphosphonic acid imprinted polymers for tyrosine phosphopeptides recognition in aqueous phase

Cited by 47 publications

References 28 publications

Advances in the development of molecularly imprinted polymers for the separation and analysis of proteins with liquid chromatography

Advances in the development of molecularly imprinted polymers for the separation and analysis of proteins with liquid chromatography

New Opportunities and Challenges of Smart Polymers in Post‐Translational Modification Proteomics

New fractionation tools targeting elusive post-translational modifications

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