史林启课题组 | ACS MACRO LETTERS
发布人：功能高分子材料教育部重点实验室 发布时间：2018/10/10 浏览次数： 120 次
Self-Assembly Molecular Chaperone to Concurrently Inhibit the Production and Aggregation of Amyloid beta Peptide Associated with Alzheimer's Disease
Huang, F (Huang, Fan)[ 1,2,3 ] ; Qu, AT (Qu, Aoting)[ 1 ] ; Yang, HR (Yang, Huiru)[ 1 ] ; Zhu, L (Zhu, Lin)[ 1 ] ; Zhou, H (Zhou, Hao)[ 4 ] ; Liu, JF (Liu, Jianfeng)[ 2,3 ] ; Long, JF (Long, Jiafu)[ 4,5 ] ; Shi, LQ (Shi, Linqi)[ 1,5 ]
MACRO LETTERS, 2018, 7(8): 983-989
Amyloid beta peptide (A beta) plays a crucial role in the pathogenesis of Alzheimer's disease (AD). Currently, decreasing A beta production and preventing A beta aggregation are thought to be important strategies in anti-AD therapy. However, inhibiting A beta production or aggregation in isolation is not sufficient to reverse the neurodegenerative process of AD patients in clinical testing. Here, a self-assembly molecular chaperone (SAMC) consisting of gamma-secretase inhibitor DAPT and mixed-shell polymeric micelles is devised, serving as a bifunctional suppressor of AD. This two-in-one combinational system can simultaneously inhibit A beta production and aggregation, which would contribute to enhancing the therapeutic effect by decreasing A beta levels. Decorating a neuron-specific RVG29 peptide onto the surface, the DAPT-incorporated SAMC can specifically target neuronal cells and, thus, will relieve the strong side effect of DAPT on normal cells. Therefore, this combination strategy holds great potential to open up an avenue for AD treatment.