Highly Efficient Extraction of Serum Peptides by Ordered Mesoporous Carbon

Qin, Hongqiang; Gao, Peng; Wang, Fangjun; Zhao, Liang; Zhu, Jun; Wang, Aiqin; Zhang, Tao; Wu, Ren’an; Zou, Hanfa

doi:10.1002/anie.201103666

Cited by 124 publications

(78 citation statements)

References 32 publications

(5 reference statements)

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“…CMK-3 was reported to have distinct hydrophobicity, and performed excellently in peptide extraction [24]. As expected, no peptides were detected in the residuary and washing solutions.…”

Section: Cmk-3 Dspesupporting

confidence: 70%

“…The procedure was performed as reported elsewhere [23,24]. Two materials, CMK-3 and MCM-41, were first washed with pure water, and then mixed with samples and shaken for 30 min.…”

Section: Dspe Using Mesoporous Materialsmentioning

confidence: 99%

“…Recently, ordered mesoporous material, MCM-41, was successfully used to selectively enrich peptides from human plasma while excluding proteins [23]. Furthermore, ordered mesoporous carbon material proved to be an outstanding alternative adsorbent for the capture of endogenous peptides from human plasma [24]. In total, 3402 peptides could be identified from only 20 μL human plasma by 2D nano-LC-MS-MS analysis.…”

Section: Introductionmentioning

confidence: 99%

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Quantitative evaluation of peptide-extraction methods by HPLC–triple-quad MS–MS

et al. 2014

Anal Bioanal Chem

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In this study, the efficiency of five peptide-extraction methods—acetonitrile (ACN) precipitation, ultrafiltration, C18 solid-phase extraction (SPE), dispersed SPE with mesoporous carbon CMK-3, and mesoporous silica MCM-41—was quantitatively investigated. With 28 tryptic peptides as target analytes, these methods were evaluated on the basis of recovery and reproducibility by using high-performance liquid chromatography-triple-quad tandem mass spectrometry in selected-reaction-monitoring mode. Because of the distinct extraction mechanisms of the methods, their preferences for extracting peptides of different properties were revealed to be quite different, usually depending on the pI values or hydrophobicity of peptides. When target peptides were spiked in bovine serum albumin (BSA) solution, the extraction efficiency of all the methods except ACN precipitation changed significantly. The binding of BSA with target peptides and nonspecific adsorption on adsorbents were believed to be the ways through which BSA affected the extraction behavior. When spiked in plasma, the performance of all five methods deteriorated substantially, with the number of peptides having recoveries exceeding 70% being 15 for ACN precipitation, and none for the other methods. Finally, the methods were evaluated in terms of the number of identified peptides for extraction of endogenous plasma peptides. Only ultrafiltration and CMK-3 dispersed SPE performed differently from the quantitative results with target peptides, and the wider distribution of the properties of endogenous peptides was believed to be the main reason.

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“…CMK-3 was reported to have distinct hydrophobicity, and performed excellently in peptide extraction [24]. As expected, no peptides were detected in the residuary and washing solutions.…”

Section: Cmk-3 Dspesupporting

confidence: 70%

“…The procedure was performed as reported elsewhere [23,24]. Two materials, CMK-3 and MCM-41, were first washed with pure water, and then mixed with samples and shaken for 30 min.…”

Section: Dspe Using Mesoporous Materialsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Quantitative evaluation of peptide-extraction methods by HPLC–triple-quad MS–MS

et al. 2014

Anal Bioanal Chem

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show abstract

“…It was utilized as trap column for automated sample injection and online multidimensional separation of protein digested samples [9], and the usage time is as long as two months due to its high rigidity and stability. Although the phosphate SCX monolithic column could be applied in high efficient online multidimensional separation for different proteome analysis [25,26], the retention strength of phosphate group is actually weaker than sulfonate group for peptide cations. It is still necessary to develop new types of sulfonate SCX monolithic columns with high rigidity to increase the retention strength.…”

Section: Introductionmentioning

confidence: 99%

Preparation of capillary hybrid monolithic column with sulfonate strong cation exchanger for proteome analysis

Zhang

Wang

et al. 2012

Journal of Chromatography A

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“…MALDI-TOF mass spectrometry is used to characterize oligomers and can provide direct and unambiguous structural information [22]. We have reported the use of this technique in peptides analysis [23]. In this study, the slow mixing of the two monomer solutions generated oligomers during the initial reaction, and this could be analyzed by MALDI-TOF mass spectrometry.…”

Section: Resultsmentioning

confidence: 99%