Published in
American Chemical Society, Journal of the American Chemical Society, 7(135), p. 2853-2862, 2013
DOI: 10.1021/ja312471h
Instytut Podstaw Informatyki, Acta Physica Polonica A, 2(114), p. 351-356, 2008
DOI: 10.12693/aphyspola.114.351
Links
- ORCID
- American Chemical Society
- Instytut Podstaw Informatyki
- [bib-pubdb1.desy.de] | PDF
- [bib-pubdb1.desy.de]
- [bib-pubdb1.desy.de] | PDF
- [bib-pubdb1.desy.de] | PDF
- [pubman.mpdl.mpg.de] | PDF
- [www.researchgate.net] | PDF
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Fano Resonance Investigation of PbTe Layers Containing Eu and Gd Ions
,
Marcus Pickhardt,
M. Pietrzyk,
Jacek Biernat,
B. Taliashvili,
R. L. Johnson,
T. Story,
Pornsuwan Soraya,
Christian Griesinger
and other authors.
Full text: Download
Abstract
Anti-aggregation drugs play an important role in therapeutic approaches for Alzheimer´s disease. Although, a large number of small molecules that inhibit the aggregation of the Tau protein have been identified, little is known about their mode of action. Here we reveal the mechanism and the nature of Tau species that are generated by interaction of Tau with the organic compound pthalocyanine tetrasulfonate (PcTS). We demonstrate that PcTS interferes with Tau filament formation by targeting the protein into soluble oligomers. A combination of NMR spectroscopy, electron paramagnetic resonance and small-angle X-ray scattering reveals that the soluble Tau oligomers contain a dynamic, non-cooperatively stabilized core with a diameter of 30 to 40 nm that is distinct from the core of Tau filaments. Our results suggest that specific modulation of the conformation of Tau is a viable strategy for reduction of pathogenic Tau deposits.