Epigallocatechin-3-gallate (EGCG)-stabilized selenium nanoparticles coated with Tet-1 peptide to reduce amyloid-β aggregation and cytotoxicity.
Alzheimer's disease (AD), the most common neurodegenerative disease, is caused by an accumulation of amyloid-β (Aβ) plaque deposits in the brains. Evidence is increasingly showing that epigallocatechin-3-gallate (EGCG) can partly protect cells from Aβ-mediated neurotoxicity by inhibiting Aβ aggregation. In order to better understand the process of Aβ 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 Aβ fibrillation and disaggregate preformed Aβ fibrils into nontoxic aggregates. In addition, we found that both EGCG@Se and Tet-1-EGCG@Se can label Aβ 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.
Department of Chemistry, Jinan University , Guangzhou 510632, China.
Jingnan
J
Zhang
Xianbo
X
Zhou
Qianqian
Q
Yu
Licong
L
Yang
Dongdong
D
Sun
Yanhui
Y
Zhou
Jie
J
Liu
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D000818:Animals; D002392:Catechin / Q000031:analogs & derivatives* / Q000737:chemistry; D002470:Cell Survival; D053768:Metal Nanoparticles / Q000737:chemistry*; D016716:PC12 Cells; D051381:Rats; D012643:Selenium / Q000737:chemistry*
D016229:Amyloid beta-Peptides; D002392:Catechin; C045651:epigallocatechin gallate; D012643:Selenium