Polymer Monoliths with Exchangeable Chemistries: Use of Gold Nanoparticles As Intermediate Ligands for Capillary Columns with Varying Surface Functionalities

Polymer Monoliths with Exchangeable Chemistries: Use of Gold Nanoparticles As Intermediate Ligands for Capillary Columns with Varying Surface Functionalities
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DOI:
10.1021/ac1015613
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发表时间:
2010-09-01
影响因子:
7.4
通讯作者:
Frechet, Jean M. J.
Frechet, Jean M. J.
中科院分区:
化学1区
文献类型:
--
作者:
Cao, Qing;Xu, Yan;Frechet, Jean M. J.

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Newly developed porous polymer monolithic capillary columns modified with gold nanoparticles coated with exchangeable functionalities allow easy switching of separation modes by a simple ligand exchange process. These columns are prepared from a poly(glycidyl methacrylate-co-ethylene dimethacrylate) monolith through reaction of its epoxide moieties with cysteamine to afford a monolith rich in surface thiol groups. Gold nanoparticles prepared via in situ reduction of chloroauric acid within the column become attached to the surface of the pores of the monolith. Alternatively, a solution of colloidal gold nanoparticles can be pumped through the thiol modified column to achieve their attachment. While the first approach is faster, it affords a lower coverage of nanoparticles than the second method, while both methods preserve the excellent hydrodynamic properties that are typical of the monolithic columns. Functionalization of the surface of the bound gold nanoparticles is then carried out using low molecular weight thiol-containing surface ligands. The dynamic nature of the bond between gold and these surface ligands enables the replacement of one surface ligand by another through a simple solution exchange process. This novel approach expands the application range of monoliths as a single column can now be used in different separations modes. Applications of the columns with exchangeable chemistries are demonstrated with the capillary electrochromatographic separation of peptides and the nano-high-pressure liquid chromatography (HPLC) separation of proteins in both reversed phase and ion exchange modes.