On-line affinity selection of histidine-containing peptides using a polymeric monolithic support for capillary electrophoresis

Vizioli, Nora Matilde; Rusell, María Lucía; Carbajal, María Laura; Carducci, C. N.; Grasselli, Mariano

doi:10.1002/elps.200410416

Cited by 50 publications

(42 citation statements)

References 28 publications

(30 reference statements)

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“…Armenta et al [263] used a glycidyl methacrylate monolith modified with protein G for the extraction of IgG from human serum, successfully demonstrating extraction from a 65 000-times diluted serum sample. Vizioli et al [264] used a similar monolith modified with iminodiacetic acid and copper for the extraction of histidine-containing peptides, with a 25-fold increase in sensitivity obtained. Tan et al [265] prepared an array of eight porous polymer monoliths in a polymer microchip for the extraction of imipramine from human urine and cytochrome P450 incubation studies.…”

Section: Spementioning

confidence: 98%

Recent advances in enhancing the sensitivity of electrophoresis and electrochromatography in capillaries and microchips

2007

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Poor sensitivity is considered to be one of the major limitations of electrophoretic separation methods, particularly when compared to traditional liquid chromatographic techniques. To address this issue, various in-line preconcentration techniques have been developed over the past 15 years, ranging in power and complexity, and there are now a number of well understood approaches routinely capable of providing a 10,000- to 100,000-fold increase in sensitivity, as well as several that can be pushed above a million. Furthermore, these have been achieved with particularly troublesome and often difficult samples, such as those having high salinity from a biological or environmental origin. This review will discuss the most common methods for improving the sensitivity of CE, CEC and microchip version of these, with particular attention to those approaches developed over the last five years.

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Section: Spementioning

confidence: 98%

Recent advances in enhancing the sensitivity of electrophoresis and electrochromatography in capillaries and microchips

2007

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“…Monolithic materials also show superiority as the supports of affinity chromatography, including IMAC adsorbents. Various miniaturized IMAC monoliths have been prepared in capillary columns with covalently bonded iminodiacetic acid (IDA) ligands for preconcentration of peptides forming chelate complexes with Cu 21 [27,28], or for enrichment of phosphopeptides by Fe 31 ions [5].…”

Section: Introductionmentioning

confidence: 99%

Monoliths with immobilized zirconium ions for selective enrichment of phosphopeptides

Wang

Duan

et al. 2011

J of Separation Science

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To meet the demands of protein phosphorylation study, immobilized zirconium ion affinity chromatography (Zr 41 -IMAC) monolith was prepared by combining UV-initiated polymerization of monolithic support and subsequent photografting in both capillary columns and microchannels. Hydrophilic poly(2-hydroxyethyl methacrylate (HEMA)-coethylene dimethacrylate (EDMA)) monolithic support was prepared under UV irradiation at the wavelength of 365 nm with monomer HEMA, crosslinker EDMA and 2,2-dimethoxy-2-phenylacetophenone as photoinitiator in 1-decanol solution, which provides good biocompatibility and permeability for biomolecule analysis. To introduce chelating ligands, such as phosphate groups, on the pore surface of monolith for metal ion immobilization, photografting of ethylene glycol methacrylate phosphate with benzophenone as the photoinitiator was performed at 254 nm for 300 s. The grafting process and metal ion immobilization can be monitored by measuring the electroosmotic flow produced by the modified monolith, providing a quantitative evaluation of post-modification. This new method for the preparation of Zr 41 -IMAC monolith simplifies the optimization of monolith preparation and avoids the time-consuming chemical modification process. Additionally, advantages include facile preparation in microdevices, easy regenerability and good reproducibility. After optimization, the microchip-based Zr 41 -IMAC monolith was used for phosphopeptide analysis and showed good selectivity in phosphopeptide enrichment with matrix-assisted laser desorption ionization mass spectrometry detection. IntroductionIn recent years, protein phosphorylation has gained much attention because of its significant roles in cellular signal transduction processes [1,2]. However, the amount of phosphorylated proteins in eukaryotic cells often exists in substoichiometry level, which makes the identification of phosphorylation sites challenging [3]. To date, mass spectrometry (MS) analysis has become an effective and commonly used method for characterization of phosphoproteins [4]. To reduce the interference of non-phosphopeptides, selective enrichment strategies, such as immobilized metal ion affinity chromatography (IMAC) [5][6][7], metal oxide affinity chromatography (MOAC) [8,9], and ion exchange chromatography [10][11][12][13], are necessary before MS analysis.Recently, chip-based system has been introduced as a promising platform for phosphopeptide analysis, due to the benefits of low sample amount, high throughput, and easy integration [14]. Several microfluidic devices have been developed by integrating phosphopeptide enrichment with other functions, such as protein alkylation and reduction [15], protein digestion [16], peptide separation and on-line interface for MS instrument [17][18][19][20], which have shown great potentials in the field of phosphoproteome research. However, in these microchip devices, phosphopeptide enrichment components are usually fabricated by packing functionalized particles, such as TiO 2 or IMAC beads, into m...

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“…Similar monolithic FS capillary columns modified with iminodiacetic acid and copper(II) ions were employed for on-line affinity capturing of histidine-containing peptides from the model peptide mixture. His-containing peptides were released from the sorbent by a 5 mM imidazole solution and separated by CZE with UV-absorption detection [52]. The same type of sorbent, monolithic column with Cu(II) iminodiacetic acid functional groups has been developed for preconcentration of low-abundance peptides and proteins from complex biological samples [53].…”

Section: Preconcentration and Preseparationmentioning

confidence: 99%

Recent developments in CE and CEC of peptides

Kašička

2007

Electrophoresis

118

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The article brings a comprehensive survey of recent developments and applications of high-performance capillary electromigration methods, zone electrophoresis, ITP, IEF, affinity electrophoresis, EKC, and electrochromatography, to analysis, preparation, and physicochemical characterization of peptides. New approaches to the theoretical description and experimental verification of electromigration behavior of peptides and to methodology of their separations, such as sample preparation, adsorption suppression, and detection, are presented. Novel developments in individual CE and CEC modes are shown and several types of their applications to peptide analysis are presented: conventional qualitative and quantitative analysis, purity control, determination in biomatrices, monitoring of chemical and enzymatical reactions and physical changes, amino acid and sequence analysis, and peptide mapping of proteins. Some examples of micropreparative peptide separations are given and capabilities of CE and CEC techniques to provide important physicochemical characteristics of peptides are demonstrated.

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On-line affinity selection of histidine-containing peptides using a polymeric monolithic support for capillary electrophoresis

Cited by 50 publications

References 28 publications

Recent advances in enhancing the sensitivity of electrophoresis and electrochromatography in capillaries and microchips

Recent advances in enhancing the sensitivity of electrophoresis and electrochromatography in capillaries and microchips

Monoliths with immobilized zirconium ions for selective enrichment of phosphopeptides

Recent developments in CE and CEC of peptides

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