Abstract
Cerebral amyloid β-peptide (Aβ) accumulation resulting from an imbalance between Aβ production and clearance is one of the most important causes in the formation of Alzheimer’s disease (AD). In order to preserve the maintenance of Aβ homeostasis and have a notable AD therapy, achieving a method to clear up Aβ plaques becomes an emerging task. Herein, we describe a self-destructive nanosweeper based on multifunctional peptide-polymers that is capable of capturing and clearing Aβ for the effective treatment of AD. The nanosweeper recognize and bind Aβ via co-assembly through hydrogen bonding interactions. The Aβ-loaded nanosweeper enters cells and upregulates autophagy thus promoting the degradation of Aβ. As a result, the nanosweeper decreases the cytotoxicity of Aβ and rescues memory deficits of AD transgenic mice. We believe that this resourceful and synergistic approach has valuable potential as an AD treatment strategy.
Highlights
Cerebral amyloid β-peptide (Aβ) accumulation resulting from an imbalance between Aβ production and clearance is one of the most important causes in the formation of Alzheimer’s disease (AD)
The emphatic pathological hallmarks of AD are extracellular deposits of selfassembled fibrils based on the amyloid β-peptide (Aβ) and intracellular neurofibrillary tangles containing hyperphosphorylated tau[4,5,6,7,8]
It has been accepted, when considering AD therapeutics, that the clearance of Aβ is the essential component in the maintenance of Aβ homeostasis
Summary
Cerebral amyloid β-peptide (Aβ) accumulation resulting from an imbalance between Aβ production and clearance is one of the most important causes in the formation of Alzheimer’s disease (AD). The nanosweeper preferentially delivers Aβ into cells and activates autophagy within them to degrade Aβ, resulting in Aβ clearance (Fig. 1). The cell viability results of MK (78.0%) and MB (80.9%) implied that they had lower anti-Aβ toxicity than M3 (Supplementary Fig. 5), which indicated that the enhanced anti-Aβ-toxicity seen with M3 originated from the synergistic effect of KLVFF and Beclin-1.
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