A novel dual-retention mechanism mixed-mode stationary phase based on silica gel functionalized with PEG 400 and succinic anhydride as the ligand was prepared and characterized by infrared spectra and elemental analysis. Because of the ligand containing PEG 400 and carboxyl function groups, it displayed hydrophobic interaction chromatography (HIC) characteristic in a high-salt-concentration mobile phase, and weak cation exchange chromatography (WCX) characteristic in a low-salt-concentration mobile phase. As a result, it can be employed to separate proteins with both WCX and HIC modes. The resolution and selectivity of the stationary phase was evaluated under both HIC and WCX modes with protein standards, and its performance was comparable to that of conventional ion-exchange chromatography and HIC columns. The results indicated that the novel dual-retention mechanism column, in many cases, could replace two individual WCX and HIC columns as a '2D column'. In addition, the mixed retention mechanism of proteins on this '2D column' was investigated with stoichiometric displacement theory for retention of solute in liquid chromatography in detail in order to understand why the dual-retention mechanism column has high resolution and selectivity for protein separation under WCX and HIC modes, respectively. Based on this '2D column', a new 2DLC technology with a single column was developed. It is very important in proteome research and recombinant protein drug production to save column expense and simplify the processes in biotechnology.
As it is difficult to prevent secondary nucleation and agglomeration during the preparation of core–shell silica microspheres, these issues have been successfully resolved in this study using template-dissolution-induced redeposition. The non-porous particles are transformed into
core–shell silica microspheres (CSSMs) in the presence of cetyltrimethylammonium bromide and octyltrimethylammonium bromide under basic conditions. The shell thickness and pore sizes of the CSSMs are controlled by adjusting the etching time and molar ratio of the template, respectively.
The CSSMs are modified using octadecyltrimethylammonium chloride to separate the mixture of alkyl benzenes, and a high column separation efficiency is achieved within two minutes. The CSSMs are used for the separation and analysis of proteins and the digests of bovine serum albumin. The chromatographic
column packed with core–shell particles affords a significantly higher separation efficiency than the commercial column. Therefore, as a chromatographic stationary phase, these core–shell particles can potentially be used for the fast separation of proteins, small solutes, and
complex samples.
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