Nano-titanium dioxide composites for the enrichment of phosphopeptides

Liang, Shih‐Shin; Makamba, Honest; Huang, Sheng; Chen, Shuhui

doi:10.1016/j.chroma.2006.03.012

Cited by 93 publications

(55 citation statements)

References 29 publications

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“…The first one is chemical reaction-based methods which include beta-elimination of the phosphate group and subsequent introduction of an affinity tag [11], and then captured by beads and released [12]. The second one is chromatography based methods which include affinity chromatography with immobilized metal ions (IMAC) [13][14][15][16][17][18][19][20][21][22][23], metal oxides such as titanium dioxide (TiO 2 ) and zirconium dioxide (ZrO 2 ) [24][25][26][27][28][29][30][31], and strong cation exchange chromatography (SCX) [32][33][34][35]. Among all of these methods, IMAC with Fe 31 is the most popular technique for the enrichment of phosphorylated peptides.…”

Section: Introductionmentioning

confidence: 99%

Large‐scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography

et al. 2008

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The mixture of phosphopeptides enriched from proteome samples are very complex. To reduce the complexity it is necessary to fractionate the phosphopeptides. However, conventional enrichment methods typically only enrich phosphopeptides but not fractionate phosphopeptides. In this study, the application of strong anion exchange (SAX) chromatography for enrichment and fractionation of phosphopeptides was presented. It was found that phosphopeptides were highly enriched by SAX and majority of unmodified peptides did not bind onto SAX. Compared with Fe 31 immobilized metal affinity chromatography (Fe 31 -IMAC), almost double phosphopeptides were identified from the same sample when only one fraction was generated by SAX. SAX and Fe 31-IMAC showed the complementarity in enrichment and identification of phosphopeptides. It was also demonstrated that SAX have the ability to fractionate phosphopeptides under gradient elution based on their different interaction with SAX adsorbent. SAX was further applied to enrich and fractionate phosphopeptides in tryptic digest of proteins extracted from human liver tissue adjacent to tumorous region for phosphoproteome profiling. This resulted in the highly confident identification of 274 phosphorylation sites from 305 unique phosphopeptides corresponding to 168 proteins at false discovery rate (FDR) of 0.96%.

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Section: Introductionmentioning

confidence: 99%

Large‐scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography

et al. 2008

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“…These studies were performed off-line with using TiO 2 microtips before LC-ESI/MS or MALDI/MS analysis of the desorbed phosphopeptides (Larsen et al, 2005a; The steps that are crucial to obtain selectivity and high recovery with TiO 2 material are (i) sample loading, (ii) unbound fraction wash, and (iii) elution of adsorbed phosphopeptides. The first is carried out under acidic conditions [i.e., 0.1% aqueous TFA or formic acid (FA; Kuroda et al, 2004;Hata et al, 2006); 0.1 M acetic acid (Pinkse et al, 2004;Liang et al, 2006)]. It was demonstrated that the addition of 2,5-dihydroxybenzoic acid (DHB; Larsen et al, 2005a;Thingholm et al, 2006;Rinalducci et al, 2006), as well as the use of high percentage of FA (2%; Schlosser, Vanselow, & Kramer, 2005) during loading and wash significantly increased the selectivity towards phosphopeptides.…”

Section: Chromatographic Selective Isolation Methodsmentioning

confidence: 98%

Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins

Temporini

Calleri

Massolini

et al. 2008

Mass Spectrometry Reviews

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The post-translational modification (PTM) of proteins is a common biological mechanism for regulating protein localization, function, and turnover. The direct analysis of modifications is required because they are not coded by genes, and thus are not predictable. Different MS-based proteomic strategies are used for the analysis of PTMs, such as phosphorylation and glycosylation, and are composed of a structural simplification step of the protein followed by specific isolation step to extract the classes of modified peptides (also called "sub-proteomes") before mass spectrometry. This specific isolation step is necessary because PTMs occur at a sub-stoichiometric level and signal suppression of the modified fractions in the mass spectrometer occurs in the presence of the more-abundant non-modified counterpart. The request of innovative analytical strategies in PTM studies is the capability to localize the modification sites, give detailed structural information on the modification, and determine the isoform composition with increased selectivity, sensitivity, and throughput. This review focuses on the description of recent integrated analytical systems proposed for the analysis of PTMs in proteins, and their application to profile the glycoproteome and the phosphoproteome in biological samples. Comments on the difficulties and usefulness of the analytical strategies are given.

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“…Highly crystalline anatase with a porous structure is desirable for p-peptide enrichment as demonstrated in previous reports. [23][24][25] A nitrogen adsorption test was used to investigate the texture of synthesized TiO 2 monolith. The N 2 adsorption-desorption isotherm of TiO 2 monolith shows a typical type II isotherm with the capillary condensation step occurring at relative pressure (P/P 0 ) .…”

Section: Resultsmentioning

confidence: 99%

Binder-Free TiO2 Monolith-Packed Pipette Tips for the Enrichment of Phosphorylated Peptides

Lei

Zhou

et al. 2016

Aust. J. Chem.

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Nano-titanium dioxide composites for the enrichment of phosphopeptides

Cited by 93 publications

References 29 publications

Large‐scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography

Large‐scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography

Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins

Binder-Free TiO2 Monolith-Packed Pipette Tips for the Enrichment of Phosphorylated Peptides

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