期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1498, 期 -, 页码 64-71出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chroma.2017.03.067
关键词
Mesoporous carbon nanoparticles; Organic-silica hybrid monolithic column; Capillary liquid chromatography (cLC); Small molecule; Protein; Peptide
资金
- National Natural Science Foundation of China [21175134, 21375125, 21505134, 21675156]
- Creative Research Group Project of National Natural Science Foundation of China [21321064]
- Instrument Developing Project of the Chinese Academy of Sciences [YZ201503]
- CAS Key Laboratory Foundation of Separation Sciences for Analytical Chemistry
- innovation program of science and research from the DICP, CAS [DICP TMSR201601]
An organic-silica hybrid monolithic capillary column was fabricated by crosslinking (3-aminopropyl)trimethoxysilane (APTMS) modified mesoporous carbon nanoparticles (AP-MCNs) with tetramethoxysilane (TMOS) and n-butyltrimethoxysilane (C4-TriMOS). Scanning electron microscopy (SEM), X-ray photoelectron spectroscopy, mercury intrusion porosimetry and inverse size-exclusion chromatography characterization proved the successful immobilization of mesoporous carbon nanoparticles (MCNs). The crosslinking of AP-MCNs into the hybrid monolithic matrix has significantly increased the reversed-phase retention of alkylbenzenes and chromatographic performance for small molecules separations in comparison with the neat one without MCNs. The resulting column efficiency of the mesoporous carbon nanoparticle-based butyl-silica hybrid monolithic column (MCN-C4-monolith) was up to ca. 116,600 N/m for the capillary liquid chromatography (cLC) separation of butylbenzene. Enhanced performance of proteins separation was achieved on the MCN-C4-monolith in comparison with the butyl-silica hybrid monolithic column without MCN (C4-monolith). The separation of peptides from bovine serum albumin (BSA) digest was carried out on the MCN-C4-monolith by capillary liquid chromatography-tandem mass spectrometry (cLC-MS/MS) with protein sequence coverage of 81.9%, suggesting its potential application in proteomics. (C) 2017 Elsevier B.V. All rights reserved.
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