Sphingomyelins as semi‐permanent capillary coatings for protein separations in CE and off‐line analysis with MALDI‐MS

Jurčić, Kristina; Yeung, Ken K.‐C.

doi:10.1002/elps.200800633

Cited by 12 publications

(11 citation statements)

References 38 publications

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“…In this case,

s = L - l

, where L is the total length of the capillary, and it is implicit that s < l and A s ≥ A l . Recovery can be estimated from:

R = {((), \frac{A_{l}}{A_{s}})}^{\frac{l}{l - s}}

It appears that this two‐point‐straight line approximation has been the approach used by all researchers in the past .…”

Section: Resultsmentioning

confidence: 99%

“…More recently though, Liu et al. and afterward Jurcic and Yeung applied Regnier concept to assess protein recovery in coated capillaries while clearly stating that recovery,

R^{'}

, was calculated from the peak area ratios obtained from the long ( A l ) and the short ( A s ) capillaries:

R^{'} = \frac{A_{l}}{A_{s}}

Unlike Eq. , this expression should result in a biased protein recovery value.…”

Section: Resultsmentioning

confidence: 99%

“…Such lack of details has resulted in diverse interpretations of the original concept. Some authors appear to interpret the method concept in a manner presumably similar to that of the original work , while others do so in a quite different fashion, as we will discuss below .…”

Section: Introductionmentioning

confidence: 99%

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Closer look at the operating definition of protein recovery in CE

2013

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Analyte recovery is an important figure to assess protein adsorption on fused-silica capillaries. In 1991 Regnier and coworkers estimated recovery by assuming the loss of analyte from adsorption and thus the decrease in peak area measured by two detectors to be proportional to the length of the capillary section between them. In this report we closely examine this concept and its adaptation to commercial CE instruments to determine protein recovery. We hypothesize that, once a steady-state migration is reached, protein adsorption is a first order process with respect to protein concentration and surface density of adsorbing sites. This hypothesis is shown to be valid over a reasonably wide range of capillary effective length and, as a result, protein recovery decreases exponentially with the migrated distance. However, unlike the traditional recovery figure obtained through a conventional spike process, protein recovery measured by this approach does not have the same merit since it is strongly dependent from capillary dimensions and applied electric field. Nevertheless, protein recovery and the slope of the logarithmic protein peak area vs. length plot are useful figures to compare protein adsorption on different capillary surfaces. Several literature reports dealing with the application of Regnier concept to calculate protein recovery are discussed.

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“…In this case,

s = L - l

, where L is the total length of the capillary, and it is implicit that s < l and A s ≥ A l . Recovery can be estimated from:

R = {((), \frac{A_{l}}{A_{s}})}^{\frac{l}{l - s}}

It appears that this two‐point‐straight line approximation has been the approach used by all researchers in the past .…”

Section: Resultsmentioning

confidence: 99%

“…More recently though, Liu et al. and afterward Jurcic and Yeung applied Regnier concept to assess protein recovery in coated capillaries while clearly stating that recovery,

R^{'}

, was calculated from the peak area ratios obtained from the long ( A l ) and the short ( A s ) capillaries:

R^{'} = \frac{A_{l}}{A_{s}}

Unlike Eq. , this expression should result in a biased protein recovery value.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Closer look at the operating definition of protein recovery in CE

2013

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“…They have shown high stability, repeatability and reproducibility in the CE‐UV and CE‐MALDI‐MS analyses of mixtures of short peptide hormones as well as large polypeptides of tryptic digests of proteins 90. Sphingomyelins (phospholipids possessing a zwitterionic head group) were used as effective semi‐permanent capillary coatings preventing wall adsorption of both cationic and anionic proteins and their enzymatic peptide fragments in their CE separations and off‐line MALDI‐MS analysis 91.…”

Section: Suppression Of Adsorption and Control Of Eofmentioning

confidence: 99%

Recent developments in CE and CEC of peptides (2009–2011)

Kašička

2011

Electrophoresis

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The review brings a comprehensive survey of the recent developments of high-performance electroseparation methods in capillary and microchip formats: zone electrophoresis, isotachophoresis, isoelectric focusing, affinity electrophoresis, electrokinetic chromatography and electrochromatography. Applications of these techniques to analysis, isolation, purification and physicochemical and biochemical characterization of peptides are described. Advances in the investigation of electromigration properties of peptides, and in the methodology of their analysis, such as sample preparation, adsorption suppression, EOF control and detection, are presented. New developments, in particular, CE and CEC modes are reported and several types of their applications to peptide analysis are described: conventional qualitative and quantitative analysis, determination in complex (bio)matrices, monitoring of chemical and enzymatical reactions and physical changes, amino acid, sequence and chiral analysis, and peptide mapping of proteins. Some micropreparative peptide separations are shown and capabilities of CE and CEC techniques to provide relevant physicochemical characteristics of peptides are demonstrated.

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“…In CEC, lipid‐based nanoparticles enabled protein separation in polymer capillaries by preventing complete adsorption to the capillary wall 28. In addition, phospholipids are among the more interesting surface modification approaches in CE 29, 30.…”

Section: Introductionmentioning

confidence: 99%

Cationic and anionic lipid‐based nanoparticles in CEC for protein separation

Nilsson

Harwigsson²,

Birnbaum

et al. 2010

Electrophoresis

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The development of new separation techniques is an important task in protein science. Herein, we describe how anionic and cationic lipid-based liquid crystalline nanoparticles can be used for protein separation. The potential of the suggested separation methods is demonstrated on green fluorescent protein (GFP) samples for future use on more complex samples. Three different CEC-LIF approaches for protein separation are described. (i) GFP and GFP N212Y, which are equally charged, were separated with high resolution by using anionic nanoparticles suspended in the electrolyte and adsorbed to the capillary wall. (ii) High efficiency (800,000 plates/m) and peak capacity were demonstrated separating GFP samples from Escherichia coli with cationic nanoparticles suspended in the electrolyte and adsorbed to the capillary wall. (iii) Three single amino-acid-substituted GFP variants were separated with high resolution using an approach based on a physical attached double-layer coating of cationic and anionic nanoparticles combined with anionic lipid nanoparticles suspended in the electrolyte. The soft and porous lipid-based nanoparticles were synthesized by a one-step procedure based on the self-assembly of lipids, and were biocompatible with a large surface-to-volume ratio. The methodology is still under development and the optimization of the nanoparticle chemistry and separation conditions can further improve the separation system. In contrast to conventional LC, a new interaction phase is introduced for every analysis, which minimizes carry-over and time-consuming column regeneration.

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Sphingomyelins as semi‐permanent capillary coatings for protein separations in CE and off‐line analysis with MALDI‐MS

Cited by 12 publications

References 38 publications

Closer look at the operating definition of protein recovery in CE

Closer look at the operating definition of protein recovery in CE

Recent developments in CE and CEC of peptides (2009–2011)

Cationic and anionic lipid‐based nanoparticles in CEC for protein separation

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