Products Cited in Publications Worldwide Ruthenium (III) Complexes that Modulate Aβ Aggregation

Ruthenium (III) Complexes that Modulate Aβ Aggregation

Yawson, Gideon Kweku

Abstract

Alzheimer’s disease (AD) is characterized by the observation of protein deposits comprised primarily of the peptide amyloid-beta (Aβ) which leads to physical changes within the brain and eventually death of an AD patient. The full-length Aβ peptide (amino acids 1-42) contains 3 histidine residues that have shown an affinity towards endogenous metal ions, a phenomenon that is exploited by metal-based drugs. Recently, two ruthenium(III) complexes NAMI-A (imidazolium [trans-RuCl4(1H-imidazole)(DMSO-S)]) and PMru20 (2-aminothiazolium [transRuCl4(2-aminothiazole)2]) were subjected to Aβ aggregation inhibition studies. Whilst it was interesting to find that both NAMI-A and PMru20 modulated Aβ aggregation, crucial questions regarding their observed activities persisted, specifically the structure-activity relationship (SAR) for the compounds. Therefore, azole-based derivatives of both complexes were prepared to determine the SAR for Ru(III) complexes to modulate the aggregation of Aβ. Analysis of the prepared Ru(III) was facilitated by three complementary methods: fluorescence spectroscopy, dynamic light scattering and transmission electron microscopy. Altogether, the results of this study have highlighted the importance of hydrogen bonding functional groups on the azole ligands having the most prominent impact on Aβ aggregation.

Keywords

Alzheimer’s Disease ; Ruthenium ; PMru20 ; NAMI-A ; Azole ; Thioflavin T ; DLS

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Aminothiazole

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Aminothiazole

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