Dual-functional selenium nanoparticles bind to and inhibit amyloid β fiber formation in Alzheimer's disease

作者：Yang, Licong; Sun, Jing; Xie, Wenjie; Liu, Yanan; Liu, Jie^*

来源：Journal of Materials Chemistry B, 2017, 5(30): 5954-5967.

DOI：10.1039/c6tb02952c

• BLOOD-BRAIN-BARRIER
• SIRNA DELIVERY
• IN-VITRO
• AGGREGATION
• PROTEIN
• AUTOPHAGY
• INDUCTION
• STABILITY
• APOPTOSIS
• PATHOLOGY

Inhibition of amyloid beta (Ab) aggregation holds considerable promise as a therapeutic strategy for Alzheimer's disease (AD). However, successful inhibition is hard to achieve due to the blood-brain barrier (BBB) and the non-selective distribution of drugs. Herein, two targeting peptides (LPFFD and TGN) were conjugated to selenium nanoparticles (SeNPs). We found that the concentration ratio of LPFFD to TGN taken as 1 : 1 could form the most effective dual-functional SeNPs (L1T1-SeNPs) for inhibiting Ab aggregation and crossing the BBB. L1T1-SeNPs can cross the BBB and have a strong affinity toward Ab species, and thus, they can efficiently suppress extracellular Ab fibrillation by disrupting hydrophobic and electrostatic interactions that are important for A beta 40 nucleation. Also, L1T1-SeNPs can suppress the Ab40 fiber mediated generation of reactive oxygen species (ROS) and their corresponding neurotoxicity in PC12 cells. In addition, L1T1-SeNPs exert synergistic effects on the inhibition of Ab aggregation and cross the BBB efficiently. Collectively, these results demonstrate that dual-functional SeNPs might be a valuable targeting system for inhibiting Ab aggregation.

• 出版日期2017-8-14
• 单位暨南大学