Analysis of synthetic derivatives of peptide hormones by capillary zone electrophoresis and micellar electrokinetic chromatography with ultraviolet-absorption and laser-induced fluorescence detection

Šolínová, Veronika; Kašička, Václav; Koval, Dušan; Barth, Tomislav; Ciencialová, Alice; Žáková, Lenka

doi:10.1016/j.jchromb.2004.01.062

Cited by 35 publications

(10 citation statements)

References 25 publications

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“…Electrophoretic mobilities were determined by CZE experiments using the mobile phase Electrophoresis 2010, 31, 933-943 composition of the LC and subsequent CEC experiments and agree well with literature data based on purely aqueous CZE buffers [58][59][60][61]. All peptides bear a positive net charge at pH 2.7.…”

supporting

confidence: 76%

Electrochromatographic retention of peptides on strong cation‐exchange stationary phases

Nischang¹,

Höltzel²,

Tallarek³

2010

Electrophoresis

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We analyze the systematic and substantial electrical field-dependence of electrochromatographic retention for four counterionic peptides ([Met5]enkephalin, oxytocin, [Arg8]vasopressin, and luteinizing hormone releasing hormone (LHRH) ) on a strong cation-exchange (SCX) stationary phase. Our experiments show that retention behavior in the studied system depends on the charge-selectivity of the stationary phase particles, the applied voltage, and the peptides' net charge. Retention factors of twice positively charged peptides ([Arg8]vasopressin and LHRH at pH 2.7) decrease with increasing applied voltage, whereas lower charged peptides (oxytocin and [Met5]enkephalin at pH 2.7, [Arg8]vasopressin and LHRH at pH 7.0) show a concomitant increase in their retention factors. The observed behavior is explained on the basis of electrical fieldinduced concentration polarization (CP) that develops around the SCX particles of the packing. The intraparticle concentration of charged species (buffer ions, peptides) increases with increasing applied voltage due to diffusive backflux from the enriched CP zone associated with each SCX particle. For twice charged and on the SCX phase strongly retained peptides the local increase in mobile phase ionic strength reduces the electrostatic interactions with the stationary phase, which explains the decrease of retention factors with increasing applied voltage and CP intensity. Lower charged and weaker retained peptides experience a much stronger relative intraparticle enrichment than the twice-charged peptides, which results in a net increase of retention factors with increasing applied voltage. The CP-related contribution to electrochromatographic retention of peptides on the SCX stationary phase is modulated by the applied voltage, the mobile phase ionic strength, and the peptides' net charge and could be used for selectivity tuning in difficult separations.

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confidence: 76%

Electrochromatographic retention of peptides on strong cation‐exchange stationary phases

Nischang¹,

Höltzel²,

Tallarek³

2010

Electrophoresis

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“…An evaluation of the optical purity of the samples was based on the corrected (migration time normalized) peak areas. [31] For chiral analysis, untreated fused silica capillaries with an outer polyimide coating of 50/375 μm id/od (Polymicro Technologies, Phoenix, AZ, USA) were used in 29/40 cm effective/total length. The background electrolyte consisted of 22 mm sodium, 35 mm phosphate buffer, pH 2.4, and a chiral selector, 6 mm heptakis(2,3-di-O-acetyl-6-O-sulfo)-β-cyclodextrin heptasodium salt (Sigma-Aldrich, cat.…”

Section: Preparation Of the Sample For The Next Round Of Pcmentioning

confidence: 99%

Preferential Crystallization of a Helicene–Viologen Hybrid – An Efficient Method to Resolve [5]Helquat Enantiomers on a 20 g Scale

et al. 2011

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The bistriflate salt of racemic [5]helquat 1 was found to form a conglomerate. Based on this finding, the preferential crystallization of this chiral helicene–viologen hybrid was developed to deliver pure enantiomers on a 20 g scale (10.5 g of each enantiomer). To the best of our knowledge, this is the largest amount of nonracemic helicene‐like compound obtained by preferential crystallization to date. The absolute configuration of the P enantiomer was confirmed by X‐ray crystal structure analysis. The chromatography‐free synthesis of racemic 1 on a multigram scale (30 g) is also presented as an entry point to this resolution study.

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“…CMEKC with 50 mM SDS pseudophase in Trisphosphate BGE, pH 8.8, has been applied for analyzing nonionogenic synthetic derivative of peptide hormone, deamino-oxytocin [140]. CMEKC has been shown to be useful also for characterization of equilibrium association constant for peptide-micelle systems involving three peptides, Leu-enkephalin, Met-enkephalin, and dipeptide Leu-Phe and two surfactants micelles, SDS and CTAB [141].…”

Section: Electrokinetic Chromatographymentioning

confidence: 99%

“…CZE and CMEKC were applied for qualitative and quantitative analysis of new synthetic derivatives of peptide neurohormones, vasopressin and oxytocin, and pancreatic hormone, human insulin and its octapetide fragment, derivatized by fluorescent probe, 4-chloro-7-nitrobenzol[1,2,5]oxadiazol (NBD) [140]. Basic ionogenic peptides were analyzed in acidic BGEs (100 mM phosphoric acid, 50 mM Tris, pH 2.25 or 0.5 M acetic acid, pH 2.5), nonionogeinic peptides were analyzed by CMEKC in 20 mM Tris, 5 mM phosphoric acid, pH 8.8 BGE with 50 mM SDS.…”

Section: Quality Control and Determination Of Puritymentioning

confidence: 99%

Recent developments in capillary electrophoresis and capillary electrochromatography of peptides

2006

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The article gives a comprehensive review on the recent developments in the applications of high-performance capillary electromigration methods, zone electrophoresis, isotachophoresis, isoelectric focusing, affinity electrophoresis, electrokinetic chromatography, and electrochromatography, to analysis, preparation, and physicochemical characterization of peptides. The article presents new approaches to the theoretical description and experimental verification of electromigration behavior of peptides, covers the methodological aspects of capillary electroseparations of peptides, such as rational selection of separation conditions, sample preparation, suppression of peptide adsorption, new developments in individual separation modes, and new designs of detection systems. Several types of applications of capillary electromigration methods 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 capillary electromigration techniques to provide important physicochemical characteristics of peptides are demonstrated.

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Analysis of synthetic derivatives of peptide hormones by capillary zone electrophoresis and micellar electrokinetic chromatography with ultraviolet-absorption and laser-induced fluorescence detection

Cited by 35 publications

References 25 publications

Electrochromatographic retention of peptides on strong cation‐exchange stationary phases

Electrochromatographic retention of peptides on strong cation‐exchange stationary phases

Preferential Crystallization of a Helicene–Viologen Hybrid – An Efficient Method to Resolve [5]Helquat Enantiomers on a 20 g Scale

Recent developments in capillary electrophoresis and capillary electrochromatography of peptides

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