Selectivity and recovery performance of phosphate-selective molecularly imprinted polymer

Kugimiya, Akimitsu; Takei, Hideo

doi:10.1016/j.aca.2007.11.025

Cited by 37 publications

(16 citation statements)

References 12 publications

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“…It is known that pH influences the binding of allylthioureas to phosphates with a maximum reached at about pH 2.5 [21]. In an MIP, better rebinding was observed at pH 4.5 than 7.5 [22]. In our experiments rebinding was better at pH 5 and 6 ( Fig.…”

Section: Uncharged Monomersupporting

confidence: 60%

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Molecular imprinting of AMP by an ionic‐noncovalent dual approach

Breton¹,

Delépée²,

Agrofoglio³

2009

J of Separation Science

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In order to mimic recognition properties of adenylate kinase, molecularly imprinted polymers (MIPs) were prepared for adenosine 5'-monophosphate (AMP), a substrate of the enzyme. Different functional monomers interacting with the phosphate moiety were tested, and the MIP giving the best specific binding of AMP was composed with one equivalent of 2-(dimethylamino)ethyl methacrylate and ten equivalents of acrylamide compared to AMP. Packed into solid phase cartridge, this polymer showed similar characteristics than the enzyme, since it was specific for AMP toward other nucleotides.

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Section: Uncharged Monomersupporting

confidence: 60%

“…Unfortunately, in this interesting paper, polymerization was achieved in solvents unable to dissolve AMP. Phosphate ion was also recovered selectively from aqueous media with polymer imprinted for phenylphosphonic acid with allythiourea as functional monomer [21,22].…”

Section: Introductionmentioning

confidence: 99%

Molecular imprinting of AMP by an ionic‐noncovalent dual approach

Breton¹,

Delépée²,

Agrofoglio³

2009

J of Separation Science

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“…As pH < 4, phosphate predominantly exists as H 3 PO 4 and H 2 PO 4 − , and H 3 PO 4 species are hardly recognized by the ion imprinted polymers, so the current change of the sensor will decrease; As 7 < pH < 10, phosphate predominantly exists as HPO 4 2− which is not matched with the imprinted cavities, and the sensor will be almost no response; As pH > 10, phosphate predominantly exists as PO 4 3− and HPO 4 2− which are also not matched with the imprinted cavities. As 4 < pH < 6, phosphate predominantly exists as H 2 PO 4 − which is consistent with the template ion, and hence the sensor has the best response in this pH value range4346. Therefore, both the functionalization of GaN-based HEMT sensor and experimental test are carried out at pH value of 5 in this work, and pH value was adjusted with HCl solution.…”

Section: Resultsmentioning

confidence: 99%

Highly selective and sensitive phosphate anion sensors based on AlGaN/GaN high electron mobility transistors functionalized by ion imprinted polymer

Jia

Chen

Liu

et al. 2016

Sci Rep

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A novel ion-imprinted electrochemical sensor based on AlGaN/GaN high electron mobility transistors (HEMTs) was developed to detect trace amounts of phosphate anion. This sensor combined the advantages of the ion sensitivity of AlGaN/GaN HEMTs and specific recognition of ion imprinted polymers. The current response showed that the fabricated sensor is highly sensitive and selective to phosphate anions. The current change exhibited approximate linear dependence for phosphate concentration from 0.02 mg L−1 to 2 mg L−1, the sensitivity and detection limit of the sensor is 3.191 μA/mg L−1 and 1.97 μg L−1, respectively. The results indicated that this AlGaN/GaN HEMT-based electrochemical sensor has the potential applications on phosphate anion detection.

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“…A phosphate-selective molecularly imprinted polymer has been prepared using 1-allyl-2-urea as a functional monomer and a diphenylphosphate template. The imprinted polymer exhibited high binding ability and selectivity for phosphate, with 70 % phosphate recovery (Kugimiya and Takei 2008 ). Recently, phosphotyrosine MIP-based receptors have been developed using two urea-based monomers and an N,O-protected p-Tyr template.…”

Section: Molecularly Imprinted Polymers (Mips)mentioning

confidence: 99%

Enrichment strategies for phosphoproteomics: state-of-the-art

Šalovská¹,

Tichý²,

Řezáčová³

et al. 2012

Reviews in Analytical Chemistry

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Protein phosphorylation is a key regulator in many biological processes, such as homeostasis, cellular signaling and communication, transcriptional and translational regulation, and apoptosis. The defects in this tightly controlled reversible posttranslational modifi cation have been described to contribute to genesis and progression of various diseases, emphasizing the importance of a systematic research of this phenomenon. Although considerable effort has been devoted to improving the analysis of phosphorylation by mass spectrometry, which is currently the method of choice to study protein phosphorylation, the detection and identifi cation of phosphorylation sites remains challenging because of the low abundance and low ionization effi cacy of phosphoproteins in comparison with nonphosphorylated proteins. To overcome this obstacle, different enrichment strategies for phosphorylated peptides/proteins have been established and optimized for subsequent mass spectrometry analysis. In this review, we will give an overview of the methods currently available for the enrichment of phosphorylated proteins and peptides including immunoprecipitation, chemical derivatization and affi nity enrichment techniques.

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Selectivity and recovery performance of phosphate-selective molecularly imprinted polymer

Cited by 37 publications

References 12 publications

Molecular imprinting of AMP by an ionic‐noncovalent dual approach

Molecular imprinting of AMP by an ionic‐noncovalent dual approach

Highly selective and sensitive phosphate anion sensors based on AlGaN/GaN high electron mobility transistors functionalized by ion imprinted polymer

Enrichment strategies for phosphoproteomics: state-of-the-art

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