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Data from Fudan University Advance Knowledge in Serine Endopeptidases (Hydrophilic polydopamine-coated magnetic graphene nanocomposites for highly...

July 14, 2014



Data from Fudan University Advance Knowledge in Serine Endopeptidases (Hydrophilic polydopamine-coated magnetic graphene nanocomposites for highly efficient tryptic immobilization)

By a News Reporter-Staff News Editor at Proteomics Weekly -- Investigators publish new report on Enzymes and Coenzymes. According to news originating from Shanghai, People's Republic of China, by NewsRx correspondents, research stated, "In this work, polydopamine-coated magnetic graphene (MG@PDA) nanocomposites were synthesized by a facile method. Trypsin was then directly immobilized on the surface of the nanocomposites through simple PDA chemistry with no need for introducing any other coupling groups."

Our news journalists obtained a quote from the research from Fudan University, "The as-made MG@PDA nanocomposites inherit not only the large surface area of graphene which makes them capable of immobilizing high amount of trypsin (up to 0.175 mg/mg), but also the good hydrophilicity of PDA which greatly improves their biocompatibility. Moreover, the strong magnetic responsibility makes them easy to be separated from the digested peptide solution when applying a magnetic field. The feasibility of the trypsin-immobilized MG@PDA (MG@PDA-trypsin) nanocomposites for protein digestion was investigated and the results indicated their high digestion efficiency in a short digestion time (10 min). In addition, the reusability and stability of the MG@PDA-trypsin nanocomposites were also tested in our work."

According to the news editors, the research concluded: "To further confirm the efficiency of MG@PDA-trypsin nanocomposites for proteome analysis, they were applied to digest proteins extracted from skimmed milk, followed by nano RPLC-ESI-MS/MS analysis, and a total of 321 proteins were identified, much more than those obtained by 16-h in-solution digestion (264 proteins), indicating the great potential of MG@PDA-trypsin nanocomposites as the supports for high-throughput proteome study."

For more information on this research see: Hydrophilic polydopamine-coated magnetic graphene nanocomposites for highly efficient tryptic immobilization. Proteomics, 2014;14(12):1457-1463. Proteomics can be contacted at: Wiley-Blackwell, 111 River St, Hoboken 07030-5774, NJ, USA. (Wiley-Blackwell - www.wiley.com/; Proteomics - onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861)

The news correspondents report that additional information may be obtained from C.Y. Shi, Fudan University, Sch Pharm, Dept. of Pharmaceut Anal, Shanghai 200433, People's Republic of China. Additional authors for this research include C.H. Deng, Y. Li, X.M. Zhang and P.Y. Yang (see also Enzymes and Coenzymes).

Keywords for this news article include: Asia, Trypsin, Shanghai, Peptide Hydrolases, Enzymes and Coenzymes, Serine Endopeptidases, 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: Proteomics Weekly


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