Pillar‐structured microchannels for on‐chip liquid chromatography: Evaluation of the permeability and separation performance

Pra, Mauro De; Malsche, Wim De; Desmet, Gert; Schoenmakers, Peter J.; Kok, Wim Th.

doi:10.1002/jssc.200600468

Cited by 39 publications

(31 citation statements)

References 16 publications

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“…These novel chromatographic systems are suitable for Lab-on-a-Chip applications that can be either packed with silica or monolithic phases or manufactured with arrays of 534j 15 Peptide Purification by Reversed-Phase Chromatography ordered pillars of silica rods with the earliest being published in 1995 [69][70][71]. These novel chromatographic systems are suitable for Lab-on-a-Chip applications that can be either packed with silica or monolithic phases or manufactured with arrays of 534j 15 Peptide Purification by Reversed-Phase Chromatography ordered pillars of silica rods with the earliest being published in 1995 [69][70][71].…”

Section: Emerging Methods For Peptide Separations For Analysis By Hypmentioning

confidence: 99%

Peptide Purification by Reversed‐Phase Chromatography

Kusebauch¹,

McBee²,

Bletz³

et al. 2010

Amino Acids, Peptides and Proteins in Organic Chemistry

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Reversed-phase high-performance liquid chromatography (RP-HPLC) has dominated peptide purification since the late 1970s due to its efficient separation and ease of use with volatile compatible buffer systems for numerous applications [1,2]. RP-HPLC separation of chains of amino acids (peptides and proteins) is based predominantly on reversible hydrophobic interactions between the amino acid side chains with the hydrophobic surface of the chromatographic stationary phase (solid particles or packings) in competition with the flowing mobile phase (chromatographic buffer or solvent). Separation is performed by binding peptides onto the hydrophobic RP stationary phase in polar conditions (e.g., water) and eluting in nonpolar solvents (e.g., organic solvent such as acetonitrile) in the presence of a pH modifying agent. As peptides bind to the stationary phase, the amount of hydrophobic area on the surface of the peptide(s) exposed to the solvent is minimized. Thus, the degree of organized water is decreased with a concomitant favorable increase in entropy of the system. For this reason, it is advantageous, under these solvent conditions, for peptides to associate with the stationary phase upon loading onto the RP-HPLC column. Mobile phase composition is then subsequently modified so that bound peptides are differentially eluted (desorbed) back into the mobile phase. The order of peptide desorption is simply based on their relative hydrophobicity (i.e., least hydrophobic proteins elute first, followed by peptides in increasing order of heir surface hydrophobicity). Peptide elution is usually performed by increasing the organic solvent concentration (either in a stepwise fashion or in a gradient manner). By these means peptides, which are concentrated or trace enriched during the binding and separation process, are eluted in a purified and concentrated form ready for collection or subsequent analysis using hyphenated techniques such as mass spectrometry.

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Section: Emerging Methods For Peptide Separations For Analysis By Hypmentioning

confidence: 99%

Peptide Purification by Reversed‐Phase Chromatography

Kusebauch¹,

McBee²,

Bletz³

et al. 2010

Amino Acids, Peptides and Proteins in Organic Chemistry

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show abstract

“…The peptides leutinizing hormone releasing hormone (LHRH, 1), angiotensin 2 (2), [val 5 ]-angiotensin 1 (3), substance P (4), renin substrate (5), momany peptide (6), insulin chain B oxidized (7), and melittin (8) were purchased from Sigma-Aldrich (Zwijndrecht, The Netherlands). Numbers between brackets correspond to the numbers used in the chromatograms to identify the peaks.…”

Section: Materials and Reagentsmentioning

confidence: 99%

“…Micromachining techniques can be used to manufacture microfluidic devices incorporating injection loops, topographic structured channels, mixers, electrospray nozzles and many more features [2][3][4][5][6][7]. So, where previously only the chromatographic column was scaled down to a smaller volume, micro technology currently offers the possibility to miniaturize the whole analytical system.…”

Section: Introductionmentioning

confidence: 99%

Methacrylate monolithic stationary phases for gradient elution separations in microfluidic devices

Pruim¹,

Öhman²,

Schoenmakers³

et al. 2011

Journal of Chromatography A

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“…On the other hand, compared with traditional packing nonporous beads column, the flow resistance can be further reduced due to the large porosity ratio (empty area/occupied area in cross section, $80% for MWCNT array, it can be calculated using: V pores ¼ p½Rp 2 À ðRp À dÞ 2 he int , with e int the internal porosity, Rp the radius of the whole pillar, h the height of the pillars, and d the thickness of the porous layer according to the estimation method in [28]). This feature can be exploited to obtain large stationary phase mass transfer rates [29]. Moreover, the laminar flow can be better maintained in such well-aligned nanostructures for decreasing the band-broadening issue by a reduction of the eddy diffusion effect, which is commonly seen in non-uniformly distributed packing structures [30].…”

Section: Introductionmentioning

confidence: 99%

Nanostructured pillars based on vertically aligned carbon nanotubes as the stationary phase in micro‐CEC

Yang

Wang

et al. 2009

Electrophoresis

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We present a micro-CEC chip carrying out a highly efficient separation of dsDNA fragments through vertically aligned multi-wall carbon nanotubes (MWCNTs) in a microchannel. The vertically aligned MWCNTs were grown directly in the microchannel to form straight nanopillar arrays as ordered and directional chromatographic supports. 1-Pyrenedodecanoic acid was employed for the surface modification of the MWCNTs' stationary phase to adsorb analytes by hydrophobic interactions. This device was used for separating dsDNA fragments of three different lengths (254, 360, and 572 bp), and fluorescence detection was employed to verify the electrokinetic transport in the MWCNT array. The micro-CEC separation of the three compounds was achieved in less than 300 s at a field strength of 66 V/cm due to superior laminar flow patterns and a lower flow resistance resulting from the vertically aligned MWCNTs being used as the stationary phase medium. In addition, a fivefold reduction of band broadening was obtained when the analyte was separated by the chromatographic MWCNT array channel instead of the CE channel. From all of the results, we suggest that an in situ grown and directional MWCNT array can potentially be useful for preparing more diversified forms of stationary phases for vertically efficient chip-based electrochromatography.

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Pillar‐structured microchannels for on‐chip liquid chromatography: Evaluation of the permeability and separation performance

Cited by 39 publications

References 16 publications

Peptide Purification by Reversed‐Phase Chromatography

Peptide Purification by Reversed‐Phase Chromatography

Methacrylate monolithic stationary phases for gradient elution separations in microfluidic devices

Nanostructured pillars based on vertically aligned carbon nanotubes as the stationary phase in micro‐CEC

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