Issue 22, 2015

Molecular “light switch” [Ru(phen)2dppzidzo]2+ monitoring the aggregation of tau

Abstract

Monitoring the aggregation of the tau protein is a key protocol for elucidating the pathogenic mechanism of Alzheimer's disease. In the present article, [Ru(phen)2dppzidzo]2+, a “light switch” ruthenium(II) complex, was presented as a new monitoring probe for the aggregation of a tau R3 peptide, the third repeat unit of the tau microtubule-binding domain. Having little impact on the aggregation process, large fixed Stokes shift and small background luminescence made the complex a better probe for monitoring the aggregation process and quantitatively detecting tau filaments compared to thioflavin S, a commonly used fluorescent dye for staining neurofibrillary tangles and monitoring tau aggregation. Furthermore, a long luminescence lifetime of this complex could also expand its potential usage in the detection of tau filaments in the presence of short-lived fluorescent backgrounds.

Graphical abstract: Molecular “light switch” [Ru(phen)2dppzidzo]2+ monitoring the aggregation of tau

Supplementary files

Article information

Article type
Communication
Submitted
10 Aug. 2015
Accepted
25 Sept. 2015
First published
25 Sept. 2015

Analyst, 2015,140, 7513-7517

Author version available

Molecular “light switch” [Ru(phen)2dppzidzo]2+ monitoring the aggregation of tau

X. Gao, L. Wang, H. Huang, L. Wang, J. Yao, S. Shi and T. Yao, Analyst, 2015, 140, 7513 DOI: 10.1039/C5AN01624J

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