Polymeric ionic liquid as a dynamic coating additive for separation of basic proteins by capillary electrophoresis

Li, Jing; Han, Haifeng; Wang, Qing; Liu, Xia; Jiang, Shengxiang

doi:10.1016/j.aca.2010.06.044

Cited by 51 publications

(31 citation statements)

References 35 publications

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“…[6,[38][39][40][41] Figure 6 showed the relationship between the ionic strength (20$100 mM) and theoretical plate number (the preparation details of the BGE were seen in Table S2, Supplemental material). The theoretical plate number increased while the ionic strength of buffer was increased from 20 to 80 mM (proteins could not be separated at 20 mM, data not shown) and reached the maximum values at 80 mM.…”

Section: Effect Of Ionic Strength Of Background Electrolyte On Proteimentioning

confidence: 99%

Application of the copolymers containing sulfobetaine methacrylate in protein separation by capillary electrophoresis

Cao

Tan

Xiang

et al. 2013

Journal of Biomaterials Science, Polymer Edition

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This study describes the formation of highly efficient antiprotein adsorption random copolymer coating of poly(N,N-dimethylacrylamide-co-sulfobetaine methacrylate) (poly(DMA-co-SBMA)) on the fused-silica capillary inner wall. Firstly, the poly(DMA-co-SBMA)s with different feed ratio (SBMA/DMA) were synthesized via the reversible addition fragmentation chain transfer polymerization. And then, X-ray photoelectron spectroscopy (XPS) and water contact angle (CA) were used to investigate the composition and hydrophilicity of poly(DMA-co-SBMA) coating formed on the glass slide surfaces. CA measurements revealed that the poly(DMA-co-SBMA) coating became more hydrophilic with the increment of feed ratio (SBMA/DMA), and at the same time, the XPS results showed that the coating ability was also increased with the increment of feed ratio. Followed, the copolymer was applied to coat the fused-silica capillary inner wall, and the coated capillary was used to separate the mixture of proteins (lysozyme, cytochrome c, ribonuclease A, and α-chymotrypsinogen A) in a pH range from 3.0 to 5.0. Under the optimum conditions, an excellent separation of basic proteins with peak efficiencies ranging from 551,000 to 1509,000 N/m had been accomplished within 10 min. Furthermore, the effect of coating composition on protein separation was also investigated through the comparison of separation efficiency achieved by using bare, PSBMA- and poly(DMA-co-SBMA)-coated capillary, respectively.

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Section: Effect Of Ionic Strength Of Background Electrolyte On Proteimentioning

confidence: 99%

Application of the copolymers containing sulfobetaine methacrylate in protein separation by capillary electrophoresis

Cao

Tan

Xiang

et al. 2013

Journal of Biomaterials Science, Polymer Edition

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“…For this purpose, several surface-active materials, mainly polymer-based such as poly(vinyl alcohol) (PVA) [5], poly(ethylene glycol) (PEG) [6], hydroxyethylcellulose [7], cationized-hydroxyethylcellulose [8], poly(vinyl pyrrolidone) [9] or different copolymers [10][11][12][13] were described in the CE and MCE literature. Other suitable surface-active compounds are surfactants [14,15], polyelectrolyte multilayers [16,17] or ionic liquids [18].…”

Section: Introductionmentioning

confidence: 99%

Poly(ethylene glycol)‐coated microfluidic devices for chip electrophoresis

Schulze

Belder

2012

Electrophoresis

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Herein, we report on a strategy for durable modification of the channel surface in microfluidic glass chips with the neutral hydrophilic-coating material poly(ethylene glycol) PEG-1M-100. Applied in microchip electrophoresis such PEG-coated devices exhibit a suppressed electroosmotic flow and reduced analyte adsorption. The PEG-coated chips were successfully applied in chip electrophoresis of FITC-labelled amines and amino acids and native proteins as well as in chiral separations. The performance of the coated chips was found to be superior compared with uncoated microchips. The coated chips exhibited high stability and the relative standard deviation of migration times in PEG-coated devices was less than 2%.

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“…The large selection of compounds that can be employed as additives of the electrolyte solution for this purpose include zwitterions, anionic or cationic ion-pairing agents, complex-forming species, chiral selectors, organic solvents, surfactants, cyclodextrins, denaturing agents, crown ethers, and ionic liquids [4][5][6][7][8][9][10][11]. The related interactions may involve either chiral on non-chiral electrostatic or/and hydrophobic interactions, as well as hydrogen bonding, ion-ion, iondipole, dipole-dipole, and ion-dipole/ion-induced-dipole interactions.…”

Section: Introductionmentioning

confidence: 99%

Interactions of Proteins with the Acidic Components of the Electrolyte Solution and Their Role in the Performance of Separations by CZE

Corradini¹,

Rossi²,

Nicoletti³

2011

Chromatographia

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This paper reports the results of a study performed to investigate the dependence of the performance of protein separation by capillary zone electrophoresis (CZE) on the anionic component of the electrolyte solutions consisting of 20 mM N,N,N 0 ,N 0 -tetramethyl-1,3-butanediamine (TMBD) titrated to either pH 4.0 or pH 6.5 with either a monoprotic or a polyprotic acid. With the exception of hydrochloric acid, the acids were selected among those commonly used as the constituents of the solutions employed for protein analysis by either HPLC or CZE. TMBD was chosen for its effectiveness at preventing the interactions of proteins with the inner wall of bare fusedsilica capillaries. The performance of separations was evaluated using four basic model proteins having pI value and molecular mass ranging from 9.5 to 11.0 and from 12,400 to 25,000 Da, respectively. It is shown that the different acids used as the components of the background electrolyte solutions, all containing the same concentration of TMBD, affect to different extents both migration time and peak shape of the tested proteins. The performance displayed by the BGE containing phosphate ions is enhanced using TMBD in combination with diethylenetriamine, an aliphatic vicinal triamine having effective buffering capacity at pH 4.0 and capability at minimizing protein-capillary wall interactions. The reported experimental evidences are discussed based on the possible interactions that the phosphate ions are known to establish with both the protein molecules and the surface of bare fused-silica capillaries.

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Polymeric ionic liquid as a dynamic coating additive for separation of basic proteins by capillary electrophoresis

Cited by 51 publications

References 35 publications

Application of the copolymers containing sulfobetaine methacrylate in protein separation by capillary electrophoresis

Application of the copolymers containing sulfobetaine methacrylate in protein separation by capillary electrophoresis

Poly(ethylene glycol)‐coated microfluidic devices for chip electrophoresis

Interactions of Proteins with the Acidic Components of the Electrolyte Solution and Their Role in the Performance of Separations by CZE

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