Immobilized metal affinity chromatography using open tubular capillary for phosphoprotein analysis: Comparison between polymer brush coating and surface functionalization

Idrissi, Khadija El; Eddarir, Saïd; Tokarski, Caroline; Rolando, Christian

doi:10.1016/j.jchromb.2011.08.005

Cited by 4 publications

(4 citation statements)

References 55 publications

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Section: 25-30mentioning

confidence: 99%

“…-IDA modified poly(glycidyl methacrylate) brushes 51 have been developed with enhanced binding capacities for phosphopeptides. However, they still lack high selectivity to the phosphopeptide enrichment in the proteomic-scale analysis.…”

Section: +mentioning

confidence: 99%

“…Due to the tunable nature of the brushes component, brush thickness, grafting density and functionality, polymer brushes are a promising candidate for biological applications. 30,[40][41][42][43][44][45][46][47][48][49][50][51][52][53] In the application of phosphopeptide enrichment, two different metal ions immobilized on the poly-(glycidyl methacrylate) brushes, 43 Fe 3+ -NTA derivatized poly-(2-hydroxyethyl methacrylate) brushes 30,46 and Fe 3+ -IDA modified poly(glycidyl methacrylate) brushes 51 have been developed with enhanced binding capacities for phosphopeptides. However, they still lack high selectivity to the phosphopeptide enrichment in the proteomic-scale analysis.…”

Section: Introductionmentioning

confidence: 99%

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A poly(ethylene glycol)-brush decorated magnetic polymer for highly specific enrichment of phosphopeptides

Zhao

Qin

et al. 2012

Chem. Sci.

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Immobilized metal affinity chromatography (IMAC) is a powerful method in phosphopeptide enrichment. However, the achievement of highly specific enrichment and sensitive detection of phosphopeptide by IMAC is still a big challenge because of the lack of high specificity and large binding capacity of conventional IMAC materials. Here, we report a novel IMAC nanoparticle to dramatically improve the enrichment specificity for the phosphopeptide by introducing a titanium phosphate moiety on a poly(ethylene glycol) methacrylate (PEG) brush decorated Fe 3 O 4 @SiO 2 core-shell nanoparticle (denoted as Fe 3 O 4 @SiO 2 @PEG-Ti 4+ IMAC nanoparticle). The thicker grafting layer of the PEG brushes has a higher chelating capacity of titanium ions. Due to the combination of the superior nonfouling property and the enhanced binding capacity of the grafted PEG brushes, the Fe 3 O 4 @SiO 2 @PEG-Ti 4+ IMAC nanoparticle demonstrated a high phosphopeptide recovery (over 70%) and low limit of detection (0.5 fmol), along with an exceptional great specificity to capture phosphopeptides from a tryptic digest of the mixture of a nonphosphorylated protein BSA and a phosphorylated protein a-casein with molar ratios of BSA/a-casein up to 2000 : 1. In the analysis of a real complex biological sample, the tryptic digests of Arabidopsis, 2447 unique phosphopeptides have been identified, showing a superior performance of the Fe 3 O 4 @SiO 2 @PEG-Ti 4+ IMAC nanoparticle than that of Fe 3 O 4 @SiO 2 -Ti 4+ (1186) and commercial TiO 2 microspheres (961). We believe that the PEG decoration for IMAC materials will be a convenient approach to significantly improve the specificity and the binding capacity of phosphopeptide enrichment.

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Section: 25-30mentioning

confidence: 99%

Section: +mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A poly(ethylene glycol)-brush decorated magnetic polymer for highly specific enrichment of phosphopeptides

Zhao

Qin

et al. 2012

Chem. Sci.

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“…Based on low concentration and signal suppression of phosphopeptides, the use of open tubular capillary columns with efficient micro‐volume scale mass transportation is expected to play a significant role in phosphopeptide enrichment by miniaturizing the sample volume and preventing contamination with nonspecific components (Bakry, Gjerde, & Bonn, ; Idrissi, Eddarir, Tokarski, & Rolando, ; Qin, Zhang, Song, Zhang, & Qian, ; Wu et al, ; Xue et al, ). For this purpose, several approaches were developed using IMAC‐based capillary columns for the enrichment of phosphopeptides (Bakry et al, ; Idrissi et al, ; Qin et al, ; Wu et al, ; Xue et al, ). Xue et al reported zirconium phosphonate‐coated open tubular capillary columns for the extraction of phosphopeptides even at concentrations of α ‐casein as low as 10 −8 m (Xue et al, ).…”

Section: Introductionmentioning

confidence: 99%

Ti (IV) attached‐phosphonic acid functionalized capillary monolith as a stationary phase for in‐syringe‐type fast and robust enrichment of phosphopeptides

Salimi

Kip

Çelikbıçak

et al. 2019

Biomedical Chromatography

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In this study, poly(vinylphosphonic acid-co-ethylene dimethacrylate), poly(VPA-co-EDMA) capillary monolith was synthesized as a starting material for obtaining a stationary phase for microscale enrichment of phosphopeptides. The chelation of active phosphonate groups with Ti (IV) ions gave a macroporous monolithic column with a mean pore size of 5.4 μm. The phosphopeptides from different sources were enriched on Ti (IV)-attached poly(VPA-co-EDMA) monolith using a syringe-pump. The monolithic capillary columns exhibited highly sensitive/selective enrichment performance with phosphoprotein concentrations as low as 1.0 fmol/mL. Six different phosphopeptides were detected with high intensity by the treatment of β-casein digest with the concentration of 1.0 fmol/mL, using Ti (IV)@poly(VPA-co-EDMA) monolith. Highly selective enrichment of phosphopeptides was also successfully carried out even at trace amounts, in a complex mixture of digested proteins (molar ratio of β-casein to bovine serum albumin, 1:1500) and three phosphopeptides were successfully detected. Four highly intense signals of phosphopeptides in human serum were also observed with high signal-to-noise ratio and a clear background after enrichment with Ti (IV)@poly(VPA-co-EDMA) monolith. It was concluded that the capillary microextraction system enabled fast, efficient and robust enrichment of phosphopeptides from microscale complex samples. The whole enrichment process was completed within 20 min, which was shorter than in the previously reported studies.KEYWORDS capillary monolith, human serum, immobilized metal affinity chromatography, phosphopeptide enrichment, syringe type microextration, vinylphosphonic acid

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Comprehensive overview of recent preparation and application trends of various open tubular capillary columns in separation science

Cheong

Ali

Kim

et al. 2013

Journal of Chromatography A

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Immobilized metal affinity chromatography using open tubular capillary for phosphoprotein analysis: Comparison between polymer brush coating and surface functionalization

Cited by 4 publications

References 55 publications

A poly(ethylene glycol)-brush decorated magnetic polymer for highly specific enrichment of phosphopeptides

A poly(ethylene glycol)-brush decorated magnetic polymer for highly specific enrichment of phosphopeptides

Ti (IV) attached‐phosphonic acid functionalized capillary monolith as a stationary phase for in‐syringe‐type fast and robust enrichment of phosphopeptides

Comprehensive overview of recent preparation and application trends of various open tubular capillary columns in separation science

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