By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Proteins. According to news reporting out of Beijing, People's Republic of China, by NewsRx editors, research stated, "Protein glycosylation regulates numerous important biological processes and plays key roles in many diseases including cancer, diabetes and inflammation. The ability to efficiently profile variation of protein glycosylation in biological samples is very useful for identifying new diagnostic biomarkers or developing new therapeutic approaches."
Our news journalists obtained a quote from the research from Beijing Proteome Research Center, "Due to the low availability of glycoprotein/glycopeptide from natural sources, enrichment before mass spectrometry (MS) analysis is usually a prerequisite. Affinity enrichment using lectins is currently one of the most widely adopted approaches. Conventionally, lectins are immobilized on solid supporting materials for sample recovery. However, the limited specific surface area, high steric hindrance and rigid nature of such supporting materials restricts lectin loading amount and results in low flexibility as well as accessibility of the immobilized lectins. Therefore, we proposed using core-shell microparticles composed of silica core and brush-like polymer chains shell for improved lectin immobilization. The surface bound brush-like polymer are synthesized by in situ growth of polymer chains from microparticle surface using surface initiated atom transfer radical polymerization (SI-ATRP). The flexible non-crosslinked polymer chains not only provide numerous binding sites, but also work as three-dimensional support for lectin immobilization, which leads to high loading amount and good accessibility of the immobilized lectin."
According to the news editors, the research concluded: "Successful enrichment which facilitated glycoprotein/glycopeptide identification is demonstrated."
For more information on this research see: Brush polymer modified and lectin immobilized core-shell microparticle for highly efficient glycoprotein/glycopeptide enrichment. Talanta, 2013;115():842-848. Talanta can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; Talanta - www.elsevier.com/wps/product/cws_home/525438)
Our news journalists report that additional information may be obtained by contacting Y.T. Pan, Beijing Inst Radiat Med, Beijing Proteome Res Center, State Key Lab Prote, Natl Center Prot Sci Beijing, Beijing 102206, People's Republic of China. Additional authors for this research include H.H. Bai, C. Ma, Y.L. Deng, W.J. Qin and X.H. Qian (see also Proteins).
Keywords for this news article include: Asia, Beijing, Glycopeptides, Glycoproteins, Glycoconjugates, People's Republic of China
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