Findings from University of Jinan Has Provided New Data on Peptides and Proteins [Epigallocatechin-3-gallate (EGCG)-Stabilized Selenium Nanoparticles Coated with Tet-1 Peptide To Reduce Amyloid-beta Aggregation and Cytotoxicity]
By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Proteins have been published. According to news reporting originating in Guangdong, People's Republic of China, by NewsRx journalists, research stated, "Alzheimer's disease (AD), the most common neurodegenerative disease, is caused by an accumulation of amyloid-beta (A beta) plaque deposits in the brains. Evidence is increasingly showing that epigallocatechin-3-gallate (EGCG) can partly protect cells from A beta-mediated neurotoxicity by inhibiting A beta aggregation."
The news reporters obtained a quote from the research from the University of Jinan, "In order to better understand the process of A beta aggregation and amyloid fibril disaggregation and reduce the cytotoxicity of EGCG at high doses, we attached EGCG onto the surface of selenium nanoparticles (EGCG@Se). Given the low delivery efficiency of EGCG@Se to the targeted cells and the involvement of selenoprotein in antioxidation and neuroprotection, which are the key factors for preventing the onset and progression of AD, we synthesized EGCG-stabilized selenium nanoparticles coated with Tet-1 peptide (Tet-1-EGCG@Se, a synthetic selenoprotein analogue), considering the affinity of Tet-1 peptide to neurons. We revealed that Tet-1-EGCG@Se can effectively inhibit A beta fibrillation and disaggregate preformed A beta fibrils into nontoxic aggregates."
According to the news reporters, the research concluded: "In addition, we found that both EGCG@Se and Tet-1-EGCG@Se can label A beta fibrils with a high affinity, and Tet-1 peptides can significantly enhance the cellular uptake of Tet-1-EGCG@Se in PC12 cells rather than in NIH/3T3 cells."
For more information on this research see: Epigallocatechin-3-gallate (EGCG)-Stabilized Selenium Nanoparticles Coated with Tet-1 Peptide To Reduce Amyloid-beta Aggregation and Cytotoxicity. ACS Applied Materials & Interfaces, 2014;6(11):8475-8487. 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 correspondents report that additional information may be obtained by contacting J.N. Zhang, Jinan Univ, Dept. of Chem, Guangzhou 510632, Guangdong, People's Republic of China. Additional authors for this research include X.B. Zhou, Q.Q. Yu, L.C. Yang, D.D. Sun, Y.H. Zhou and J. Liu (see also Proteins).
Keywords for this news article include: Asia, Amyloid, Minerals, Proteins, Selenium, Guangdong, Chalcogens, Nanoparticle, Nanotechnology, Emerging Technologies, People's Republic of China
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