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Amino acid and ionic liquid modified polyhedral oligomeric silsesquioxane-based hybrid monolithic column for high-efficiency capillary liquid chromatography
•Amino acid and ionic liquid modified POSS-based monolithic column was developed.•The column exhibited reduced hydrophobicity with introduction of polar L-cysteine.•Polar compounds could be efficiently separated under RPLC mode.•Intact proteins exhibited strong retention and good separation selectiv...
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Published in: | Journal of Chromatography A 2018-10, Vol.1572, p.82-89 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | •Amino acid and ionic liquid modified POSS-based monolithic column was developed.•The column exhibited reduced hydrophobicity with introduction of polar L-cysteine.•Polar compounds could be efficiently separated under RPLC mode.•Intact proteins exhibited strong retention and good separation selectivity.
In this study, a novel amino acid and ionic liquid dual organically functionalized reagents modified polyhedral oligomeric silsesquioxane methacryl substituted (POSS-MA) based hybrid monolithic column (POSS-VBI-Cys) was designed and reported. With amino acid L-cysteine and ionic liquid 1-vinyl-3-butylimidazolium bromide as dual monomers, POSS-MA as the crosslinker, the new POSS-VBI-Cys hybrid monolithic column could be facilely fabricated via the “one-pot” free radical copolymerization and thiol-ene click reaction. Because of the introduction of polar amino acid L-cysteine, the new POSS-VBI-Cys column exhibited attenuated hydrophobicity in reversed-phase liquid chromatography separation. Polar amides, nucleosides and nucleic acid bases displayed strong retention on the POSS-VBI-Cys column and could be successfully separated. Furthermore, the new POSS-VBI-Cys column displayed good separation selectivity for model glycoproteins and non-glycoproteins mixture and it was also successfully used for the purification and separation of TARG1 protein from its originally expressed sample. In the future research, we will further exploit its performances for separation of intact proteins and in-depth proteome applications. |
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ISSN: | 0021-9673 |
DOI: | 10.1016/j.chroma.2018.08.045 |