Comparison of selectivities of reversed-phase high-performance liquid chromatography, capillary zone electrophoresis and micellar capillary electrophoresis in the separation of neurohypophyseal peptides and analogues

Sutcliffe, Nick; Corran, Patrick H.

doi:10.1016/0021-9673(93)80061-c

Cited by 32 publications

(5 citation statements)

References 37 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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supporting

confidence: 76%

Electrochromatographic retention of peptides on strong cation‐exchange stationary phases

Nischang¹,

Höltzel²,

Tallarek³

2010

Electrophoresis

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“…The CMC, evaluated using the shift in UV/Vis absorption maximum of methylene blue, was found to be around 8 mM. This value was in good agreement with data from other studies [17]. At concentrations above the CMC, CHAPS monomers interact by the backto-back bile salt model and form micelles with a small aggregation number (2±15 monomers per micelle) [26].…”

Section: Chaps-mekcsupporting

confidence: 88%

“…Unfortunately, the dynorphin analogs are cationic (pI > 10) in the normal working range for electrophoresis experiments and thus strongly ion-paired with SDS by nonspecific electrostatic forces leading to no separation. The unsuitability of micelles of opposite charge for separating peptides by MEKC has been noted previously [16,17].…”

Section: Sds-mekcmentioning

confidence: 76%

Micellar electrokinetic chromatography separations of dynorphin peptide analogs

Fürtös‐Matei¹,

Day²,

St‐Pierre³

et al. 2000

Electrophoresis

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“…These peptides were also separated by MEKC in 20 mM tetraborate BGE with micellar pseudophase formed by sodium dodecylsulfate (SDS), pH 9.2 [11,12]. Oxytocin, vasopressin and other neurohypophyseal nonapeptides were determined by MEKC in four different micellar systems-with cationic, anionic, zwitterionic and neutral micellar constituents [14]. Chiral separations of dalargin analogs with d-and l-isomers of phenylalanine in the fourth position in peptide chain were performed in 50 mM phosphate buffer, pH 2.5 with 10 mM ␤-cyclodextrin [12].…”

Section: Introductionmentioning

confidence: 99%

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

Šolínová

Kašička

Koval

et al. 2004

Journal of Chromatography B

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Comparison of selectivities of reversed-phase high-performance liquid chromatography, capillary zone electrophoresis and micellar capillary electrophoresis in the separation of neurohypophyseal peptides and analogues

Cited by 32 publications

References 37 publications

Electrochromatographic retention of peptides on strong cation‐exchange stationary phases

Electrochromatographic retention of peptides on strong cation‐exchange stationary phases

Micellar electrokinetic chromatography separations of dynorphin peptide analogs

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

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