Oxidized dextran facilitated synthesis of a silica-based concanavalin a material for lectin affinity enrichment of glycoproteins/glycopeptides

Liu, Yujie; Fu, Dongmei; Yu, Long; Xiao, Yuansheng; Peng, Xiaojun; Liang, Xinmiao

doi:10.1016/j.chroma.2016.05.093

Cited by 46 publications

(19 citation statements)

References 41 publications

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“…In a recent study, a silica‐based concanavalin A (SiO 2 ‐ODex Con A) material with oxidized dextran as the spacer has been synthesized to enrich glycoproteins/glycopeptides in egg white and human serum . Also, conventional (3‐glycidoxypropyl) triethoxysilane was used to synthesize another silica‐based Con A material (SiO 2 ‐Ald Con A).…”

Section: Methodologies Used To Reduce the Complexity Of Proteomic Sammentioning

confidence: 99%

Liquid‐phase based separation systems for depletion, prefractionation, and enrichment of proteins in biological fluids and matrices for in‐depth proteomics analysis—An update covering the period 2014–2016

Rassi

Puangpila

2016

Electrophoresis

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This review article is an update of our previous one by C. Puangpila, E. Mayadunne, and Z. El Rassi, Electrophoresis 2015, 36, 238-252. Similarly to the previous article, this review has two main topics, including (i) proteomic sample preparation (e.g., depletion of high-abundance proteins, reduction of the protein dynamic concentration range, and enrichment of a particular subproteome), and (ii) the subsequent chromatographic and/or electrophoretic prefractionation prior to protein separation and identification by LC-MS/MS. More than 70 papers published in the period extending from mid-2014 to the present have been reviewed. Although an effort was made to yield a comprehensive review article, one may safely state that this review article is by no means thorough, and the aim was to rather provide a concise description of the latest developments in the field.

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Section: Methodologies Used To Reduce the Complexity Of Proteomic Sammentioning

confidence: 99%

Liquid‐phase based separation systems for depletion, prefractionation, and enrichment of proteins in biological fluids and matrices for in‐depth proteomics analysis—An update covering the period 2014–2016

Rassi

Puangpila

2016

Electrophoresis

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“…Lectin-based SPE can be performed by gravity flow (Nie et al, 2013;Bag et al, 2014;Bériot et al, 2014;Tan et al, 2014;Yang et al, 2014;Noro et al, 2015Noro et al, , 2015Liu et al, 2016a, Liu et al, 2016bAndrade-Silva et al, 2016;Peixoto et al, 2016;Zhang et al, 2016;Cotton et al, 2017;Azevedo et al, 2018;Chang et al, 2019;Ideo et al, 2020) or with low-pressure conditions (Jung and Cho, 2013;Yang et al, 2014Yang et al, , 2014Ruiz-May et al, 2014;King et al, 2017;Totten et al, 2018). However, spin column formats have also been proposed, which necessitate a centrifugation step in order to perform the washing and elution steps (Ahn et al, 2014;Kontro et al, 2014;Tan et al, 2014Tan et al, , 2015Zhang et al, 2015).…”

Section: Solid Phase Extraction With Commercial Lectin-based Sorbentsmentioning

confidence: 99%

Recent Advances in Lectin-Based Affinity Sorbents for Protein Glycosylation Studies

Goumenou

Delaunay

Pichon

2021

Front. Mol. Biosci.

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Glycosylation is one of the most significant post-translational modifications occurring to proteins, since it affects some of their basic properties, such as their half-life or biological activity. The developments in analytical methodologies has greatly contributed to a more comprehensive understanding of the quantitative and qualitative characteristics of the glycosylation state of proteins. Despite those advances, the difficulty of a full characterization of glycosylation still remains, mainly due to the complexity of the glycoprotein and/or glycopeptide mixture especially when they are present in complex biological samples. For this reason, various techniques that allow a prior selective enrichment of exclusively glycosylated proteins or glycopeptides have been developed in the past and are coupled either on- or off- line with separation and detection methods. One of the most commonly implemented enrichment methods includes the use of lectin proteins immobilized on various solid supports. Lectins are a group of different, naturally occurring proteins that share a common characteristic, which concerns their affinity for specific sugar moieties of glycoproteins. This review presents the different formats and conditions for the use of lectins in affinity chromatography and in solid phase extraction, including their use in dispersive mode, along with the recent progress made on either commercial or home-made lectin-based affinity sorbents, which can lead to a fast and automated glycosylation analysis.

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“…Concanavalin A (ConA), the most widely used lectin, has a high affinity in binding the high mannose core in N-glycans (Y. Liu et al, 2016;Ohyama, Kasai, Nomoto, & Inoue, 1985). Wheat germ agglutinin (WGA) tend to specifically binds to sialic acid and N-acetyl-glucosamine (Bhavanandan & Katlic, 1979;Nagata & Burger, 1974;K.…”

Section: Enrichment With Lectin Affinity Chromatography (Lac)mentioning

confidence: 99%

Isolation and characterization of glycosylated neuropeptides

Liu

Cao

2019

Methods in Enzymology

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Glycosylation is one of the most ubiquitous and complex post-translational modifications (PTMs). It plays pivotal roles in various biological processes. Studies at the glycopeptide level are typically considered as a downstream work resulting from enzymatic digested glycoproteins. Less attention has been focused on glycosylated endogenous signaling peptides due to their low abundance, structural heterogeneity and the lack of enabling analytical tools. Here, protocols are presented to isolate and characterize glycosylated neuropeptides utilizing nanoflow liquid chromatography coupled with mass spectrometry (LC-MS). We first demonstrate how to extract neuropeptides from raw tissues and perform further separation/cleanup before MS analysis. Then we describe hybrid MS methods for glycosylated neuropeptides profiling and site-specific analysis. We also include recommendations for data analysis to identify glycosylated neuropeptides in crustaceans where a complete neuropeptide database is still lacking. Other strategies and future directions are discussed to provide readers with alternative approaches and further unravel biological complexity rendered by glycosylation.

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Oxidized dextran facilitated synthesis of a silica-based concanavalin a material for lectin affinity enrichment of glycoproteins/glycopeptides

Cited by 46 publications

References 41 publications

Liquid‐phase based separation systems for depletion, prefractionation, and enrichment of proteins in biological fluids and matrices for in‐depth proteomics analysis—An update covering the period 2014–2016

Liquid‐phase based separation systems for depletion, prefractionation, and enrichment of proteins in biological fluids and matrices for in‐depth proteomics analysis—An update covering the period 2014–2016

Recent Advances in Lectin-Based Affinity Sorbents for Protein Glycosylation Studies

Isolation and characterization of glycosylated neuropeptides

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