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Fabrication of an ionic‐liquid‐based polymer monolithic column and its application in the fractionation of proteins from complex biosamples
Author(s) -
Zhang Doudou,
Zhang Qian,
Bai Ligai,
Han Dandan,
Liu Haiyan,
Yan Hongyuan
Publication year - 2018
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.201701369
Subject(s) - monolith , monolithic hplc column , chromatography , ionic liquid , porosimetry , chemistry , polymerization , polymer , methacrylate , ethylene glycol dimethacrylate , adsorption , chemical engineering , ethylene glycol , desorption , polyethylene glycol , materials science , high performance liquid chromatography , porosity , methacrylic acid , organic chemistry , porous medium , engineering , catalysis
An ionic‐liquid‐based polymer monolithic column was synthesized by free radical polymerization within the confines of a stainless‐steel column (50 mm × 4.6 mm id). In the processes, ionic liquid and stearyl methacrylate were used as dual monomers, ethylene glycol dimethacrylate as the cross‐linking agent, and polyethylene glycol 200 and isopropanol as co‐porogens. Effects of the prepolymerization solution components on the properties of the resulting monoliths were studied in detail. Scanning electron microscopy, nitrogen adsorption–desorption measurements, and mercury intrusion porosimetry were used to investigate the morphology and pore size distribution of the prepared monoliths, which showed that the homemade ionic‐liquid‐based monolith column possessed a relatively uniform macropore structure with a total macropore specific surface area of 44.72 m 2 /g. Compared to a non‐ionic‐liquid‐based monolith prepared under the same conditions, the ionic‐liquid‐based monolith exhibited excellent selectivity and high performance for separating proteins from complex biosamples, such as egg white, snailase, bovine serum albumin digest solution, human plasma, etc., indicating promising applications in the fractionation and analysis of proteins from the complex biosamples in proteomics research.