Development of Ru-polypyridyl complexes for real-time monitoring of Aβ oligomers and inhibition of Aβ fibril formation

Xian Chen; Jiaoyang Wang; Zhenzhuo Mo; Lu Han; Kaiqing Cheng; Cheng Xie; Genyan Liu; Lijun Jiang; Kai Wang; Jie Pan

doi:10.1039/D3BM01929B

Development of Ru-polypyridyl complexes for real-time monitoring of Aβ oligomers and inhibition of Aβ fibril formation†

Xian Chen,^a Jiaoyang Wang,^a Zhenzhuo Mo,^a Lu Han,^a Kaiqing Cheng,^a Cheng Xie,^c Genyan Liu,*^c Lijun Jiang,*^b Kai Wang*^a and Jie Pan

*^a

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* Corresponding authors

^a College of Health Science and Engineering, Hubei University, Wuhan 430062, P. R. China
E-mail: j.pan@hubu.edu.cn

^b College of Life Sciences, Central China Normal University, Wuhan 430062, P. R. China

^c Hubei Key Laboratory of Novel Reactor and Green Chemical Technology, School of Chemical Engineering and Pharmacy, Wuhan Institute of Technology, Wuhan, PR China

Abstract

The aggregation of amyloid-β (Aβ) is one of the important pathological markers of Alzheimer's disease. Ruthenium(II) complexes have good stability, low cytotoxicity, a high fluorescence quantum yield, and a good Stokes shift as fluorescent probes. Based on this, we constructed a fluorescent probe for in vivo real-time imaging and inhibition of Aβ-fibril formation using a complex of Ru polypyridine with organic fluorophores (N,N-dimethylaniline) and hydrophobic peptides (KLVFF). DLS and TEM studies have shown that Ru-YH has an inhibitory effect on the fibrotic aggregation of Aβ. Both in vivo and in vitro studies have shown that Ru-WJ and Ru-YH can quickly cross the blood–brain barrier and successfully detect Aβ in early (2.5-month old) transgenic mouse models. In summary, we have explored the potential of Ru complex based biological probes for early diagnosis and inhibition of AD.

Biomaterials Science

Development of Ru-polypyridyl complexes for real-time monitoring of Aβ oligomers and inhibition of Aβ fibril formation†

Abstract

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Development of Ru-polypyridyl complexes for real-time monitoring of Aβ oligomers and inhibition of Aβ fibril formation

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