TiO2-functionalized mesoporous materials for sensitive analysis of multi-phosphopeptides

Weichao Guo; Jingjing Wan; Kun Qian; Chengzhong Yu; Jilie Kong; Pengyuan Yang; Baohong Liu

doi:10.1007/s11426-011-4344-5

TiO₂-functionalized mesoporous materials for sensitive analysis of multi-phosphopeptides

Weichao Guo
, Jingjing Wan
, Kun Qian
, Chengzhong Yu
, Jilie Kong
, Pengyuan Yang
, Baohong Liu^*

^*Corresponding author for this work

Fudan University

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Protein phosphorylation as one of the most important post-translational modifications in mammalian cells regulates numerous biological processes. Here we propose a novel strategy for the selective isolation and sensitive analysis of multi-phosphopeptides based on TiO₂-gratfed mesoporous materials, in which MCM-41 and SBA-15 were chosen as the hard templates. The commercialized IMAC and TiO₂ nanopartices were further investigated in the phosphopeptide analysis for comparison. The enrichment efficiency was evaluated and measured by MALDI-TOF mass spectrometry. The results indicated that both TiO₂-SBA-15 and TiO₂-MCM-41 exhibited the preferential affinity to multi-phosphopeptides compared with the other two widely used strategies. The mesoporous TiO₂ based protocol showed highly selective and sensitive properties, where phosphopeptides could be identified at femtomole.

Original language	English
Pages (from-to)	1327-1333
Number of pages	7
Journal	Science China Chemistry
Volume	54
Issue number	8
DOIs	https://doi.org/10.1007/s11426-011-4344-5
State	Published - Aug 2011
Externally published	Yes

Keywords

TiO
enrichment
mesoporous materials
multi-phosphopeptides

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10.1007/s11426-011-4344-5

Cite this

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title = "TiO2-functionalized mesoporous materials for sensitive analysis of multi-phosphopeptides",

abstract = "Protein phosphorylation as one of the most important post-translational modifications in mammalian cells regulates numerous biological processes. Here we propose a novel strategy for the selective isolation and sensitive analysis of multi-phosphopeptides based on TiO2-gratfed mesoporous materials, in which MCM-41 and SBA-15 were chosen as the hard templates. The commercialized IMAC and TiO2 nanopartices were further investigated in the phosphopeptide analysis for comparison. The enrichment efficiency was evaluated and measured by MALDI-TOF mass spectrometry. The results indicated that both TiO2-SBA-15 and TiO2-MCM-41 exhibited the preferential affinity to multi-phosphopeptides compared with the other two widely used strategies. The mesoporous TiO2 based protocol showed highly selective and sensitive properties, where phosphopeptides could be identified at femtomole.",

keywords = "TiO, enrichment, mesoporous materials, multi-phosphopeptides",

author = "Weichao Guo and Jingjing Wan and Kun Qian and Chengzhong Yu and Jilie Kong and Pengyuan Yang and Baohong Liu",

year = "2011",

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doi = "10.1007/s11426-011-4344-5",

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}

TY - JOUR

T1 - TiO2-functionalized mesoporous materials for sensitive analysis of multi-phosphopeptides

AU - Guo, Weichao

AU - Wan, Jingjing

AU - Qian, Kun

AU - Yu, Chengzhong

AU - Kong, Jilie

AU - Yang, Pengyuan

AU - Liu, Baohong

PY - 2011/8

Y1 - 2011/8

N2 - Protein phosphorylation as one of the most important post-translational modifications in mammalian cells regulates numerous biological processes. Here we propose a novel strategy for the selective isolation and sensitive analysis of multi-phosphopeptides based on TiO2-gratfed mesoporous materials, in which MCM-41 and SBA-15 were chosen as the hard templates. The commercialized IMAC and TiO2 nanopartices were further investigated in the phosphopeptide analysis for comparison. The enrichment efficiency was evaluated and measured by MALDI-TOF mass spectrometry. The results indicated that both TiO2-SBA-15 and TiO2-MCM-41 exhibited the preferential affinity to multi-phosphopeptides compared with the other two widely used strategies. The mesoporous TiO2 based protocol showed highly selective and sensitive properties, where phosphopeptides could be identified at femtomole.

AB - Protein phosphorylation as one of the most important post-translational modifications in mammalian cells regulates numerous biological processes. Here we propose a novel strategy for the selective isolation and sensitive analysis of multi-phosphopeptides based on TiO2-gratfed mesoporous materials, in which MCM-41 and SBA-15 were chosen as the hard templates. The commercialized IMAC and TiO2 nanopartices were further investigated in the phosphopeptide analysis for comparison. The enrichment efficiency was evaluated and measured by MALDI-TOF mass spectrometry. The results indicated that both TiO2-SBA-15 and TiO2-MCM-41 exhibited the preferential affinity to multi-phosphopeptides compared with the other two widely used strategies. The mesoporous TiO2 based protocol showed highly selective and sensitive properties, where phosphopeptides could be identified at femtomole.

KW - TiO

KW - enrichment

KW - mesoporous materials

KW - multi-phosphopeptides

UR - https://www.scopus.com/pages/publications/80052659791

U2 - 10.1007/s11426-011-4344-5

DO - 10.1007/s11426-011-4344-5

M3 - 文章

AN - SCOPUS:80052659791

SN - 1674-7291

VL - 54

SP - 1327

EP - 1333

JO - Science China Chemistry

JF - Science China Chemistry

IS - 8

ER -

TiO₂-functionalized mesoporous materials for sensitive analysis of multi-phosphopeptides

Abstract

Keywords

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