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Findings on Peptides and Proteins Reported by Investigators at Fudan University (Fe3O4/PVIM-Ni2+ Magnetic Composite Microspheres for Highly Specific...

July 22, 2014



Findings on Peptides and Proteins Reported by Investigators at Fudan University (Fe3O4/PVIM-Ni2+ Magnetic Composite Microspheres for Highly Specific Separation of Histidine-Rich Proteins)

By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Peptides and Proteins. According to news reporting out of Shanghai, People's Republic of China, by NewsRx editors, research stated, "Integration of the advantages of immobilized metal-ion affinity chromatography (IMAC) and magnetic microspheres is considered as an ideal pathway for quick and convenient separation of his-tagged proteins, but rare reports concern the natural histidine-rich proteins. In this article, a novel route was presented to fabricate magnetic microspheres composed of a high-magnetic-response magnetic supraparticle (Fe3O4) core and a Ni2+-immobilized cross-linked polyvinyl imidazole (PVIM) shell via reflux-precipitation polymerization."

Our news journalists obtained a quote from the research from Fudan University, "The unique as-prepared Fe3O4/PVIM-Ni2+ microspheres possessed uniform flower-like structure, high magnetic responsiveness, abundant binding sites, and very easy synthesis process. Taking advantage of the pure PVIM-Ni2+ interface and high Ni2+ loading amount, the microspheres exhibited remarkable selectivity, excellent sensitivity, large enrichment capacity, and high recyclability in immobilization and separation of his-tagged recombinant proteins. More interestingly, it was found that the Fe3O4/PVIM-Ni2+ microspheres also showed excellent performance for removal of the natural histidine-rich bovine serum albumin (BSA) from the complex real sample of fetal bovine serum due to the exposed histidine residues."

According to the news editors, the research concluded: "Considering their multiple merits, this new type of Fe3O4/PVIM-Ni2+ nanomaterial displays great potential in enriching low-abundant his-tagged proteins or removing high-abundant histidine-rich natural proteins for proteomic analysis."

For more information on this research see: Fe3O4/PVIM-Ni2+ Magnetic Composite Microspheres for Highly Specific Separation of Histidine-Rich Proteins. ACS Applied Materials & Interfaces, 2014;6(11):8836-8844. ACS Applied Materials & Interfaces can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; ACS Applied Materials & Interfaces - www.pubs.acs.org/journal/aamick)

Our news journalists report that additional information may be obtained by contacting Y.T. Zhang, Fudan University, Adv Mat Lab, Shanghai 200433, People's Republic of China. Additional authors for this research include D. Li, M. Yu, W.F. Ma, J. Guo and C.C. Wang (see also Peptides and Proteins).

Keywords for this news article include: Asia, Shanghai, Amino Acids, Peptides and Proteins, 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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