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Findings in the Area of Peptides and Proteins Reported from Chinese Academy of Sciences (Boronate Affinity Monolith with a Gold Nanoparticle-Modified...

August 19, 2014



Findings in the Area of Peptides and Proteins Reported from Chinese Academy of Sciences (Boronate Affinity Monolith with a Gold Nanoparticle-Modified Hydrophilic Polymer as a Matrix for the Highly Specific Capture of Glycoproteins)

By a News Reporter-Staff News Editor at Life Science Weekly -- Fresh data on Proteins are presented in a new report. According to news reporting from Beijing, People's Republic of China, by NewsRx journalists, research stated, "As low abundance is the great obstacle for glycoprotein analysis, the development of materials with high efficiency and selectivity for glycoprotein enrichment is a prerequisite in glycoproteome research. Herein, we report a new kind of hydrophilic boronate affinity monolith by attaching 4-mercaptophenylboronic acid (MPBA) with 2-mercaptoethylamine (MPA) on the gold nanoparticle-modified poly(glycidyl methacrylate-co-poly(ethylene glycol) diacrylate)) monolith for glycoprotein enrichment."

The news correspondents obtained a quote from the research from the Chinese Academy of Sciences, "With poly(ethylene glycol) diacrylate as the cross-linker and the further modification of gold nanoparticles, the matrix has advantages of good hydrophilicity and enhanced surface area, which are beneficial to improve the enrichment selectivity and efficiency for glycoproteins. The attachment of MPBA and MPA provide intramolecular B-N coordination, which could further enhance the specificity of glycoprotein capture. Such a boronate affinity monolith was applied to enrich horseradish peroxidase (HRP) from the mixture of HRP and bovine serum albumin (BSA), and high selectivity was obtained even at a mass ratio of 1:1000. In addition, the binding capacity of ovalbumin on such monolith reached 390 mu g g(-1). Furthermore, the average recovery of HRP on the prepared affinity monoliths was (84.8 +/- 1.9)%, obtained in three times enrichment with the same column. Finally, the boronate affinity monolith was successfully applied for the human-plasma glycoproteome analysis."

According to the news reporters, the research concluded: "As a result, 160 glycoproteins were credibly identified from 9 mu g of human plasma, demonstrating the great potential of such a monolith for large-scale glycoproteome research."

For more information on this research see: Boronate Affinity Monolith with a Gold Nanoparticle-Modified Hydrophilic Polymer as a Matrix for the Highly Specific Capture of Glycoproteins. Chemistry-A European Journal, 2014;20(28):8737-8743. Chemistry-A European Journal can be contacted at: Wiley-V C H Verlag Gmbh, Boschstrasse 12, D-69469 Weinheim, Germany (see also Proteins).

Our news journalists report that additional information may be obtained by contacting C. Wu, Univ Chinese Academy Sci, Beijing 100039, People's Republic of China. Additional authors for this research include Y. Liang, Q. Zhao, Y.Y. Qu, S. Zhang, Q. Wu, Z. Liang, L.H. Zhang and Y.K. Zhang.

Keywords for this news article include: Asia, Beijing, Glycoproteins, Nanotechnology, Glycoconjugates, Gold Nanoparticles, Emerging Technologies, People's Republic of China

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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