Novel tetrazole-functionalized ion exchanger for weak cation-exchange chromatography of proteins

Lei, Genhu; Xiong, Xiaohu; Wei, Yinmao; Zheng, Xiaohui; Jian, Zheng

doi:10.1016/j.chroma.2008.02.031

Cited by 26 publications

(14 citation statements)

References 31 publications

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“…In IR spectra, nitrilefunctionalized silica exhibited a strong absorption at 2,232 cm -1 due to CN stretching vibration, but after the reaction with NaN 3 , there appeared two important bands, strong absorption at 1,647 cm -1 , and a medium absorption at 1,407 cm -1 , which were attributed to the characteristic frequencies of tetrazole groups. These results were in good agreement with the values in the literature [19]. Element analysis showed the change of nitrogen content of the bonded silica (Table 1).…”

Section: Characterization Of Tetrazole-functionalized Silicasupporting

confidence: 94%

“…1, was prepared according to the methods reported in the previous publication [19]. Briefly, dry silica was first modified with c-glycidoxypropyltrimethoxysilane to obtain epoxide-activated silica.…”

Section: Synthesis Of Tetrazole-functionalized Silicamentioning

confidence: 99%

“…Based on this property, tetrazole-functionalized silica as ion exchanger was reported for biopolymer separation in our previous work [18,19]. Since tetrazole also has strong polarity and the ability to form multiple hydrogen bonding [20], tetrazole-functionalized silica was expected to act as a potential HILIC stationary phase.…”

Section: Introductionmentioning

confidence: 98%

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Tetrazole-Functionalized Silica for Hydrophilic Interaction Chromatography of Polar Solutes

et al. 2011

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In this work, tetrazole-functionalized stationary phase was prepared with nitrile-modified silica by an ammonium-catalyzed (3 ? 2) azide-nitrile cycloaddition reaction. The prepared stationary phase was used for separation of nucleobases and nucleosides by hydrophilic interaction chromatography (HILIC) mode. A typical HILIC mechanism was observed at higher content of acetonitrile ([85%, v/v) in the mobile phase. The retention mechanism of the column was investigated by the models used for describing partitioning and surface adsorption through adjustment ratio of water in the mobile phase, and by the influence of salt concentration, buffer pH, and temperature on the retention of solutes. The results illustrated that the surface adsorption through hydrogen bonding dominated the retention behavior of nucleobases/ nucleosides under HILIC mode. From the separation ability, the tetrazole-functionalized stationary phase could become a valuable alternative for the separation of the compounds concerned.

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Section: Characterization Of Tetrazole-functionalized Silicasupporting

confidence: 94%

Section: Synthesis Of Tetrazole-functionalized Silicamentioning

confidence: 99%

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Tetrazole-Functionalized Silica for Hydrophilic Interaction Chromatography of Polar Solutes

et al. 2011

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“…After the column was saturated, it was flushed with 20 mM phosphate buffer (pH 7. [57,58], but is almost two times higher than that obtained for a tetrazole-functionalized ion exchanger [59]. This comparable dynamic binding capacity is presumably due to the high amount of SPMA used in the copolymerization.…”

Section: Dynamic Binding Capacitymentioning

confidence: 47%

Polymeric strong cation‐exchange monolithic column for capillary liquid chromatography of peptides and proteins

Chen

Tolley

Lee³

2009

J of Separation Science

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A strong cation-exchange (SCX) monolithic stationary phase was prepared in 75 microm id capillaries by direct in situ polymerization of sulfopropyl methacrylate and polyethylene glycol diacrylate in a ternary porogen system consisting of methanol, cyclohexanol, and water. The resulting monolith exhibited good dynamic binding capacity, fast kinetic adsorption of proteins, and high permeability. The monolith had a dynamic binding capacity of approximately 52 mg/mL of column volume for lysozyme and cytochrome C. The monolith was evaluated for SCX capillary LC of synthetic peptides, natural peptides, and protein standards. Fast separation of proteins was achieved in less than 4 min. The average peak capacity for peptides was 28 using a relatively steep gradient when hydrophobic interactions were suppressed with 40% acetonitrile.

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“…And multifunctional separation mechanism including ion exchange was also observed on poly(ethylene glycol) (PEG)-based stationary phase [9]. In addition, a novel tetrazolefunctionalized weak cation-exchanger for the analysis of protein has been developed, in which the tetrazole ring functions as ion exchange site [10].…”

Section: Introductionmentioning

confidence: 98%

Separation of inorganic anions on a triazole‐functionalized ion exchanger in ion chromatography

Zhang

Liu

Wei

et al. 2011

J of Separation Science

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The retention behavior of inorganic anions on a triazole-based stationary phase was first examined in ion chromatography. It was initially designed for hydrophilic interaction liquid chromatography and was simply prepared by introducing the triazole groups onto the surface of silica gel via click chemistry. Effective separation of common inorganic anions, including iodate, chloride, bromide, nitrate and iodide, was achieved with Na(2)SO(4) eluent. The logarithm of the retention factor of analytes was observed to be linear with the logarithm of the eluent concentration, and the slopes of the plots were almost the same as those of the ideal theoretical value. The eluent pH value in the range of 3.4-7.0 had little effect on the separation. The utility of the column was demonstrated for the determination of UV-absorbing anions in saliva and tap water.

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Novel tetrazole-functionalized ion exchanger for weak cation-exchange chromatography of proteins

Cited by 26 publications

References 31 publications

Tetrazole-Functionalized Silica for Hydrophilic Interaction Chromatography of Polar Solutes

Tetrazole-Functionalized Silica for Hydrophilic Interaction Chromatography of Polar Solutes

Polymeric strong cation‐exchange monolithic column for capillary liquid chromatography of peptides and proteins

Separation of inorganic anions on a triazole‐functionalized ion exchanger in ion chromatography

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