Separation of eleven angiotensin II analogs by capillary electrophoresis with a nonionic surfactant in acidic media

Matsubara, Naoko; Koezuka, Kiyohiro; Terabe, Shigeru

doi:10.1002/elps.1150160194

Cited by 30 publications

(10 citation statements)

References 12 publications

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“…In addition, several communications have appeared dealing with the use of both neutral and zwitterionic surfactants, but here too the accent was on micellar electrokinetic chromatography, i.e., on the ability of these compounds to modulate the separation of peptides (and in general of hydrophobic compounds), via adsorption/interaction of the analyte with the detergent micelle. Thus, Greve et al [67], Issaq et al [68], van de Goor et al [69] and Yeung and Lucy [70] have used zwitterionic surfactants for improving the separation of different peptide mixtures; Swedberg [71] adopted nonionic and zwitterionic detergents with heptapeptides; Matsubara et al [72] and Matsubara and Terabe [73] utilized Tween 20 and Polysorbate 20 for optimizing the separation of closely related angiotensin II analogues.…”

Section: Behavior Of Surfactantsmentioning

confidence: 99%

The state of the art of dynamic coatings

et al. 2001

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The present review highlights the mechanisms of action and efficiency of three major classes of dynamic coatings so far adopted in capillary electrophoresis: (i) amines to oligo-amines, (ii) neutral synthetic and natural polymers, and (iii) neutral and zwitter-ionic surfactants. Their merits and efficacy have been explored in depth via a novel quantitation technique consisting of eluting, by frontal analysis, any adsorbed proteinaceous material, which can then be correctly quantified as a peak as it moves in front of the detector window. This is achieved by loading sodium dodecyl sulfate (SDS) micelles onto the cathodic side and migrating them electrophoretically into the capillary lumen, where they efficiently sweep any adsorbed polypeptide material. It is found that a common trend, for all quenchers, is linked to a hydrophobicity scale: the more hydrophobic the inhibitor, the better it minimizes potential interactions of macromolecules with the wall. This seems to be true for all the classes of dynamic modifiers tested. Finally, we describe a novel, dynamic to static quencher: it is a quaternary piperazine, bearing a reactive iodine atom at the end of a butyl tail (N(methyl-N-omega-iodo-butyl),N'-methyl piperazine). This molecule first binds to the wall, at alkaline pH values, via ionic and hydrogen bonds. Once docked onto the wall, the reactive tail forms a covalent link with the silica surface, to which it then remains permanently affixed.

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Section: Behavior Of Surfactantsmentioning

confidence: 99%

The state of the art of dynamic coatings

et al. 2001

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“…As the components of bacitracin carry positive charge, it was found that the acidic buffer (pH 2.5) was essential to reduce the adsorption of the analyte on the capillary wall. In literature, PAPS [25] and nonionic surfactant [26,27] were found to be useful for the separation of peptides with closely related structures with MEKC. In the present case, it was found that PAPS offered a better selectivity than Brij 35.…”

Section: Methods Developmentmentioning

confidence: 99%

Analysis of bacitracin by micellar electrokinetic capillary chromatography with mixed micelle in acidic solution

et al. 2001

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A method used for quantitative analysis of bacitracin with micellar electrokinetic capillary chromatography (MEKC) is described. As capillary zone electrophoresis gave poor separation selectivity, MEKC was preferable. It was found that a zwitterionic surfactant, 3-(N,N-dimethylhexadecylammonium)-propanesulfonate (PAPS) gave the best selectivity among the several surfactants studied. As the analytes tend to adsorb onto the capillary wall due to their positive charge, an acidic solution composed of Tris-phosphate buffer at pH 2.5 was necessary to diminish such adsorption. The peak tailing caused by relatively strong ion pair interaction between the analyte and PAPS micelle could be reduced by adding nonionic surfactant Brij 35 to the PAPS solution. This phenomenon is possibly explained by a mixed micelle mechanism. In order to obtain the optimal conditions and to test the method robustness, a central composite experimental design was performed. The optimal conditions are as follows: 44 cm length of fused-silica capillary with 50 microm inner diameter, 90 mM Tris-phosphate buffer (pH 2.5) containing 17 mM PAPS and 0.3% w/v-Brij 35, 18 kV applied voltage, UV detection at 192 nm and 25 degrees C column temperature. Under the optimal conditions, more than 50 peaks could be obtained in 30 min. The method had a linearity range from 1 to 0.05 mg/mL (concentration of bacitracin A). The limit of quantitation (LOQ) and limit of detection (LOD) were 0.005 and 0.0012 mg/mL, respectively.

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“…With peptides differing in hydrophobicity, the common approach to effect a separation is the implementation of a hydrophobic interaction by using micelles: zwitterionic, e.g., CHAPS [21]; neutral, e.g., Brij 35 [22], Tween 20 [23], octyl glucoside [24]; or charged [21]. Especially impressive was the separation by Fürtös-Matei et al [21] of 13 Ala-scan dynorphin analogues with CHAPS as additive.…”

Section: Hydrophobic Interaction Mechanism: Mekcmentioning

confidence: 99%

Capillary electrophoresis of synthetic peptide standards varying in charge and hydrophobicity

2003

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A mixture of eight structurally closely related synthetic peptides as capillary electrophoretic (CE) standards is introduced. The almost identical mass-to-charge ratio of the standards, coupled with their random-coil (i.e., no secondary structure) nature, offer a potent analytical test for CE to separate peptides varying only subtly in hydrophobicity. Parameters varied to effect a separation included background electrolyte concentration, temperature, applied voltage in capillary zone electrophoresis (CZE in uncoated capillaries), as well as the introduction of hydrophobic mechanisms to the separation either through the use of micelles or C8-coated capillaries. Our step-by-step approach culminated in an optimized combination of a CZE mechanism for separation of differently charged peptide groups (based on common mass-to-charge ratio) and an ion-pairing mechanism (effecting a separation within each group of identically charged peptides), which we have termed ion-interaction CZE or II-CZE. The study clearly shows how the peptide standards allow an excellent assessment of the resolving power of CE.

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Separation of eleven angiotensin II analogs by capillary electrophoresis with a nonionic surfactant in acidic media

Cited by 30 publications

References 12 publications

The state of the art of dynamic coatings

The state of the art of dynamic coatings

Analysis of bacitracin by micellar electrokinetic capillary chromatography with mixed micelle in acidic solution

Capillary electrophoresis of synthetic peptide standards varying in charge and hydrophobicity

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