Ti4+-immobilized hierarchically porous zirconium-organic frameworks for highly efficient enrichment of phosphopeptides

Yang, He; Zheng, Qi; Lin, Zian

doi:10.1007/s00604-021-04760-x

Cited by 17 publications

(4 citation statements)

References 42 publications

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“…Detailed comparison of enrichment performance with other reported MOF-based materials is listed in Table . ,,,− The comparison consisted of sensitivity, selectivity, recovery, and biological application. It was clear that Fe 3 O 4 @MIL-101-CoPc showed better performance in aspects of selectivity and recovery for the enrichment of low-abundance phosphopeptides.…”

Section: Resultsmentioning

confidence: 99%

Cobalt Phthalocyanine-Modified Magnetic Metal–Organic Frameworks for Specific Enrichment of Phosphopeptides

Jiang,

Wu,

et al. 2024

ACS Biomater. Sci. Eng.

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For mass spectrometry (MS)-based phosphoproteomics studies, sample pretreatment is an essential step for efficient identification of lowabundance phosphopeptides. Herein, a cobalt phthalocyanine-modified magnetic metal−organic framework (MOF) (Fe 3 O 4 @MIL-101-CoPc) was prepared and applied to enrich phosphopeptides before MS analysis. Fe 3 O 4 @ MIL-101-CoPc exhibited an excellent magnetic response (74.98 emu g −1 ) and good hydrophilicity (7.75°), which were favorable for the enrichment. Fe 3 O 4 @ MIL-101-CoPc showed good enrichment performance with high selectivity (1:1:5000), sensitivity (0.1 fmol), reusability (10 circles), and recovery (91.3%). Additionally, the Fe 3 O 4 @MIL-101-CoPc-based MS method was able to successfully detect 827 phosphopeptides from the A549 cell lysate, demonstrating a high enrichment efficiency (89.3%). This study promotes the application of postfunctionalized MOFs for phosphoproteomics analysis.

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Section: Resultsmentioning

confidence: 99%

Cobalt Phthalocyanine-Modified Magnetic Metal–Organic Frameworks for Specific Enrichment of Phosphopeptides

Jiang,

Wu,

et al. 2024

ACS Biomater. Sci. Eng.

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“…As a novel porous material, metal–organic frameworks (MOFs) have features of regular porous structure, tunable properties, and high surface area. − In MOFs, a periodic skeleton structure is formed by a combination of organic ligands and metal ions. The unsaturated metal ions can provide affinity sites for phosphoprotein adsorption. , However, MOFs still have some drawbacks, such as poor stability and single adsorption site, restricting the further application in proteomics. , Therefore, there is still an urgent need to design a new pattern of MOF-based porous materials for proteomic analysis.…”

Section: Introductionmentioning

confidence: 99%

“…The unsaturated metal ions can provide affinity sites for phosphoprotein adsorption. 11,12 However, MOFs still have some drawbacks, such as poor stability and single adsorption site, restricting the further application in proteomics. 13,14 Therefore, there is still an urgent need to design a new pattern of MOF-based porous materials for proteomic analysis.…”

Section: Introductionmentioning

confidence: 99%

Effective Enrichment of Phosphopeptides Using Magnetic Polyoxometalate-Based Metal–Organic Frameworks

Jiang,

Wu,

et al. 2023

ACS Biomater. Sci. Eng.

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“…Over the past years, a plethora of methods has been developed for the enrichment and MS analysis of phosphopeptides [10][11][12], such as immobilized metal ion affinity chromatography [13,14] and metal oxide affinity chromatography [15,16]. Taking advantage of the high affinity of chelated metal ions or metal oxides to the negatively charged phosphate groups, these methods allowed for extensive phosphoproteomics analysis covering tens of thousands of phosphorylation sites in large-scale studies.…”

Section: Introductionmentioning

confidence: 99%

Highly efficient enrichment of intact phosphoproteins by a cadmium ion‐based co‐precipitation strategy

Fan

Yao

et al. 2022

J of Separation Science

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Selective separation and enrichment of phosphoproteins are essential for understanding their important functions in almost all cellular processes. Here, taking advantage of the feature that cadmium ion (Cd2+) has an overwhelming preference for phosphates, we developed a robust and simple Cd2+ co‐precipitation strategy for the selective isolation of intact phosphoproteins. After evaluating the feasibility of Cd2+ in phosphoprotein precipitation, we compared the washing protocols for the removal of non‐specific binding proteins and then used the best‐performing protocol for the isolation of phosphoproteins from different complex samples. It was found that phosphoproteins can be specifically enriched from artificial protein mixtures containing α‐casein, β‐casein, and bovine serum albumin or plasma, in which bovine serum albumin or plasma were served as interferences with very high molar ratios. Applying this method to enrich phosphoproteins from complex cell lysates, a high specificity was confirmed by western blotting analysis with a phosphoprotein‐specific kit. Finally, we successfully applied this method to the purification of caseins from drinking milk, highlighting its potential application in the studies where purified phosphoproteins were required. In a word, this Cd2+ co‐precipitation method enables universal and effective capture, enrichment, and detection of intact phosphoproteins, making it a powerful tool for the comprehensive analysis of the phosphoproteome.

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Ti4+-immobilized hierarchically porous zirconium-organic frameworks for highly efficient enrichment of phosphopeptides

Cited by 17 publications

References 42 publications

Cobalt Phthalocyanine-Modified Magnetic Metal–Organic Frameworks for Specific Enrichment of Phosphopeptides

Cobalt Phthalocyanine-Modified Magnetic Metal–Organic Frameworks for Specific Enrichment of Phosphopeptides

Effective Enrichment of Phosphopeptides Using Magnetic Polyoxometalate-Based Metal–Organic Frameworks

Highly efficient enrichment of intact phosphoproteins by a cadmium ion‐based co‐precipitation strategy

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