Recent applications of capillary electrochromatography

Vanhoenacker, Gerd; Bosch, Tine Van den; Rozing, Gerard P.; Sandra, Pat

doi:10.1002/1522-2683(200111)22:19<4064::aid-elps4064>3.0.co;2-9

Cited by 69 publications

(18 citation statements)

References 180 publications

(94 reference statements)

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“…Recent results focusing on the improvement of column technology expanded the selectivity of this miniaturized technique, that at present is able to perform rapid separations of many classes of compounds also including charged species such as chiral and nonchiral drugs, metabolites, food additives, pesticides, protein digest, peptides, etc. [4][5][6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

CEC separation of insect oostatic peptides using a strong‐cation‐exchange stationary phase

Rocco¹,

Aturki²,

D’Orazio³

et al. 2007

Electrophoresis

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The separation of several insect oostatic peptides (IOPs) was achieved by using CEC with a strong-cation-exchange (SCX) stationary phase in the fused-silica capillary column of 75 mm id. The effect of organic modifier, ionic strength, buffer pH, applied voltage, and temperature on peptides' resolution was evaluated. Baseline separation of the studied IOPs was achieved using a mobile phase containing 100 mM pH 2.3 sodium phosphate buffer/ water/ACN (10:20:70 v/v/v). In order to reduce the analysis time, experiments were performed in the short side mode where the stationary phase was packed for 7 cm only. The selection of the experimental parameters strongly influenced the retention time, resolution, and retention factor. An acidic pH was selected in order to positively charge the analyzed peptides, the pI's of which are about 3 in water buffer solutions. A good selectivity and resolution was achieved at pH ,2.8; at higher pH the three parameters decreased due to reduced or even zero charge of peptides. The increase in the ionic strength of the buffer present in the mobile phase caused a decrease in retention factor for all the studied compounds due to the decreased interaction between analytes and stationary phase. Raising the ACN concentration in the mobile phase in the range 40-80% v/v caused an increase in both retention factor, retention time, and resolution due to the hydrophilic interactions of IOPs with free silanols and sulfonic groups of the stationary phase.

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Section: Introductionmentioning

confidence: 99%

CEC separation of insect oostatic peptides using a strong‐cation‐exchange stationary phase

Rocco¹,

Aturki²,

D’Orazio³

et al. 2007

Electrophoresis

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“…However, to exploit the full potentials of CEC, further progress is needed in the area of column technology. Most stationary phases used in CEC have been those based on silica microparticles packed in capillaries (for recent reviews, see [1][2][3]), and more recently those composed of monoliths (for recent reviews see [4][5][6]). The recent interest in monolithic stationary phases has been triggered in part by the various problems encountered in the use of microparticulate stationary phases including (i) the difficulty of reproducibly packing small particles into a capillary, (ii) the low permeability of capillaries packed with small particles, which bring about long washing time for equilibration and solvent change, (iii) frequent bubble formation, and (iv) the need for retaining frits which increase the fragility of the capillary and also increase bubble formation.…”

Section: Introductionmentioning

confidence: 99%

Capillary electrochromatography with monolithic silica column: I. Preparation of silica monoliths having surface‐bound octadecyl moieties and their chromatographic characterization and applications to the separation of neutral and charged species

Allen

Rassi

2003

Electrophoresis

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Monolithic silica columns with surface-bound octadecyl (C18) moieties have been prepared by a sol-gel process in 100 microm ID fused-silica capillaries for reversed-phase capillary electrochromatography of neutral and charged species. The reaction conditions for the preparation of the C18-silica monoliths were optimized for maximum surface coverage with octadecyl moieties in order to maximize retention and selectivity toward neutral and charged solutes with a sufficiently strong electroosmotic flow (> 2 mm/s) to yield rapid analysis time. Furthermore, the effect of the pore-tailoring process on the silica monoliths was performed over a wide range of treatment time with 0.010 M ammonium hydroxide solution in order to determine the optimum time and conditions that yield mesopores of narrow pore size distribution that result in high separation efficiency. Under optimum column fabrication conditions and optimum mobile phase composition and flow velocity, the average separation efficiency reached 160 000 plates/m, a value comparable to that obtained on columns packed with 3 microm C18-silica particles with the advantages of high permeability and virtually no bubble formation. The optimized monolithic C18-silica columns were evaluated for their retention properties toward neutral and charged analytes over a wide range of mobile phase compositions. A series of dimensionless retention parameters were evaluated and correlated to solute polarity and electromigration property. A dimensionless mobility modulus was introduced to describe charged solute migration and interaction behavior with the monolithic C18-silica in a counterflow regime during capillary electrochromatography (CEC )separations. The mobility moduli correlated well with the solute hydrophobic character and its charge-to-mass ratio.

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“…This mode is also commonly used to estimate the molecular weight of proteins using Ferguson plots (Ferguson, 1964). Adding micelles like SDS (micellar electrokinetic capillary chromatography; MEKC) to background electrolytes and using a separation channel containing particles or monoliths (capillary electrochromatography; CEC) are two alternative methods for separating proteins, which are based on partition of proteins in mobile phase and (pseudo) stationary phase (Bruin, 2000;Vanhoenacker et al, 2001;Jing et al, 2002;Molina and Silva, 2002;Holland and Leigh, 2003;Kasicka, 2003).…”

Section: Separation Mechanisms and Detection Approachesmentioning

confidence: 99%

Advanced Capillary and Microchip Electrophoretic Techniques for Proteomics

Changa¹,

Huanga²,

Chiou³

et al. 2004

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This review focuses on rapid, efficient, and sensitive characterization of the proteome by capillary electrophoresis (CE) and microchip capillary electrophoresis (MCE) in conjunction with laser-induced fluorescence (LIF). A number of advanced CE-LIF and MCE-LIF techniques, including on-column concentration techniques, on-line chemical reaction and enzyme-assay techniques, integrated microdevices, and high-efficiency multidimensional separation techniques that have been developed within the past few years, are capable for the analysis of trace proteins in biological samples and/or in single cells. These powerful techniques also show great potential for drug screening and diagnosis. The basic principle of each technique and its advantages and shortcomings for proteomics studies are discussed in detail. We also highlight the importance of techniques that possess improved analytical sensitivity, sample throughput, and quantitation capabilities for identifying the complexities and dynamics of the proteome expressed by cells, tissues, or an organism.

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Recent applications of capillary electrochromatography

Cited by 69 publications

References 180 publications

CEC separation of insect oostatic peptides using a strong‐cation‐exchange stationary phase

CEC separation of insect oostatic peptides using a strong‐cation‐exchange stationary phase

Capillary electrochromatography with monolithic silica column: I. Preparation of silica monoliths having surface‐bound octadecyl moieties and their chromatographic characterization and applications to the separation of neutral and charged species

Advanced Capillary and Microchip Electrophoretic Techniques for Proteomics

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