Research Article

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2018, 11(4): 1987–1997

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https://doi.org/10.1007/s12274-017-1815-9

Rational design of a “sense and treat” system to target amyloid aggregates related to Alzheimer’s disease

Zhi Du, Nan Gao (*), Yijia Guan, Chao Ding, Yuhuan Sun, Jinsong Ren, and Xiaogang Qu (*)

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Laboratory of Chemical Biology and State Key laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Changchun 130022, China

Keywords: Alzheimer’s disease (AD), amyloid-β peptide, oligomer detection, magnetothermal modality, “sense and treat”
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ABSTRACT The aggregation of amyloid-β peptide (Aβ) is implicated in the pathology of Alzheimer’s disease (AD), and Aβ oligomers are considered the most toxic species. Therefore, the detection and clearance of Aβ oligomers are crucial for the theranostic strategies for AD. However, effective methods for the detection of Aβ oligomers are rare, and only few of the oligomer-specific sensors have therapeutic functions as well. Recent studies have demonstrated that the toxicity of Aβ oligomers is related to the number of exposed hydrophobic residues. In this study, an oligomer-specific fluorescent probe, which was based on the hydrophobic regions that are exposed on Aβ oligomer surfaces was designed and synthesized. For improving the ability to recognize Aβ oligomers, the in situ treatment of AD symptoms and the ability to penetrate the blood-brain barrier, the probe and KLVFF peptide (an Aβ-target peptide) were modified on the surfaces of magnetic nanoparticles (MNP@NFP-pep). This complex could detect Aβ oligomers specifically, and achieve the wireless deep magnetothermally mediated disaggregation of Aβ aggregates with an alternating magnetic field. This work provides new insights into the development of a “sense and treat” system for AD therapy.
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Rational design of a “sense and treat” system to target amyloid aggregates related to Alzheimer’s disease. Nano Res. 2018, 11(4): 1987–1997 https://doi.org/10.1007/s12274-017-1815-9

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