Magnetic bead-based hydrophilic interaction liquid chromatography for glycopeptide enrichments

Yeh, Chia Hao; Chen, Shu Hui; Li, Ding Tzai; Lin, Hong Ping; Huang, Hung Jen; Chang, Chi I.; Shih, Wen L.; Chern, Chi Liang; Shi, Fong Ku; Hsu, Jue‐Liang

doi:10.1016/j.chroma.2011.12.057

Cited by 53 publications

(29 citation statements)

References 46 publications

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“…For this purpose, a number of enrichment approaches have been developed, including lectin affinity, 386–387 hydrazide coupling, 388 HILIC, 389–390 and boronic acid affinity. 391–392 Among these strategies, lectin-affinity is the most widely used due to its high specificity.…”

Section: Ptm Analysis By Mass Spectrometrymentioning

confidence: 99%

Protein Analysis by Shotgun/Bottom-up Proteomics

et al. 2013

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Section: Ptm Analysis By Mass Spectrometrymentioning

confidence: 99%

Protein Analysis by Shotgun/Bottom-up Proteomics

et al. 2013

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“…More recently, an alternative separation strategy using magnetic beads coated with a hydrophilic interaction liquid chromatography (HILIC) stationary phase has also been described (29). Although the HILIC approach appears to be quite advantageous, the beads are not currently commercially available; however, the preparation does not seem to require extensive expertise (29).…”

Section: Emerging Methods Supporting Glycopeptide Analysismentioning

confidence: 99%

Glycopeptide Analysis, Recent Developments and Applications

Desaire

2013

Molecular & Cellular Proteomics

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Glycopeptide-based analysis is used to inform researchers about the glycans on one or more proteins. The method's key attractive feature is its ability to link glycosylation information to exact locations (glycosylation sites) on proteins. Numerous applications for glycopeptide analysis are known, and several examples are described herein. The techniques used to characterize glycopeptides are still emerging, and recently, research focused on facilitating aspects of glycopeptide analysis has advanced significantly in the areas of sample preparation, MS fragmentation, and automation of data analysis. These recent developments, described herein, provide the foundation for the growth of glycopeptide analysis as a blossoming field. Molecular & Cellular

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“…This study also showed that enrichment of N ‐linked glycoproteins using hydrazide chemistry showed significant loss of peptides when compared to TiO 2 and HILIC strategy, possibly due to the extended enrichment scheme . Interestingly, a recent study using magnetic bead‐based HILIC nanoparticles showed high specificity and recovery (95–100%) for the enrichment of glycoproteins from urine; 85 N ‐glycosylation sites in 53 glycoproteins . Another TiO 2 ‐based capturing strategy has been utilized in combination with click chemistry for the purification of O ‐Glc N Acylated peptides from HeLa cells and mouse brain tissues by Gal N Az enzymatic labeling and cycloaddition of a phospho‐alkyne, prior to TiO 2 chromatography .…”

Section: Glycoprotein Enrichment Strategies For Proteomics Analysismentioning

confidence: 83%

Glycocapture‐based proteomics for secretome analysis

2013

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Protein glycosylation represents the most abundant extracellular posttranslational modification in multicellular organisms. These glycoproteins unequivocally comprise the major biomolecules involved in extracellular processes, such as growth factors, signaling proteins for cellular communication, enzymes, and proteases for on- and off-site processing. It is now known that altered protein glycosylation is a hallmark event in many different pathologies. Glycoproteins are found mostly in the so-called secretome, which comprises classically and nonclassically secreted proteins and protein fragments that are released from the cell surface through ectodomain shedding. Due to biological complexity and technical difficulty, comparably few studies have taken an in-depth investigation of cellular secretomes using system-wide approaches. The cellular secretomes are considered to be a valuable source of therapeutic targets and novel biomarkers. It is not surprising that many existing biomarkers, including biomarkers for breast, ovarian, prostate, and colorectal cancers are glycoproteins. Focused analysis of secreted glycoproteins could thus provide valuable information for early disease diagnosis, and surveillance. Furthermore, since most secreted proteins are glycosylated and glycosylation predominantly targets secreted proteins, the glycan/sugar moiety itself can be used as a chemical "handle" for the targeted analysis of cellular secretomes, thereby reducing sample complexity and allowing detection of low abundance proteins in proteomic workflows. This review will focus on various glycoprotein enrichment strategies that facilitate proteomics-based technologies for the quantitative analysis of cell secretomes and cell surface proteomes.

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Magnetic bead-based hydrophilic interaction liquid chromatography for glycopeptide enrichments

Cited by 53 publications

References 46 publications

Protein Analysis by Shotgun/Bottom-up Proteomics

Protein Analysis by Shotgun/Bottom-up Proteomics

Glycopeptide Analysis, Recent Developments and Applications

Glycocapture‐based proteomics for secretome analysis

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