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Screening π-Extended Ruthenium(II) Complexes for the Photoinduced Oxidative Modulation of Amyloid-β Peptide

Grace Leech¹, Isabella Bayly¹, Alisher Talgatov²

¹Department of Chemistry, Simon Fraser University, Burnaby, BC V5A-1S6, Canada.

Inorganic Chemistry

|December 25, 2025

Summary

This summary is machine-generated.

Controlling amyloid-β (Aβ) aggregation is key for Alzheimer's disease (AD) therapy. New photoactivatable ruthenium complexes, particularly Ru1, use light to generate singlet oxygen, promoting Aβ degradation and offering a novel therapeutic approach.

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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Area of Science:

Biochemistry
Materials Science
Neuroscience

Background:

Alzheimer's disease (AD) is linked to amyloid-β (Aβ) peptide aggregation.
Current therapeutic strategies aim to control Aβ aggregation.
Developing targeted methods to modify Aβ aggregation is crucial.

Purpose of the Study:

To introduce photoactivatable ruthenium(II) complexes (Ru1-8) for controlling Aβ aggregation.
To investigate the mechanism of Aβ modification via singlet oxygen generation.
To evaluate the therapeutic potential of these complexes in Alzheimer's disease models.

Main Methods:

Synthesis and characterization of photoactivatable Ru(II) complexes.
Photoactivation studies using UV-Vis spectroscopy and transmission electron microscopy (TEM).
Biochemical assays including bicinchoninic acid (BCA) quantification, Western blotting, and proteinase-K digestion.

Main Results:

Ru(II) complexes, especially Ru1, efficiently generate singlet oxygen upon light activation.
Photoactivation rapidly induces Aβ1-42 aggregation into amorphous species.
Amorphous aggregates are more susceptible to proteolysis compared to canonical fibrils.
Ru1 demonstrates both preventive and disruptive activity against Aβ aggregation.

Conclusions:

Photoactivatable Ru(II) complexes offer a light-controlled method to modulate Aβ aggregation.
Ru1 effectively redirects Aβ aggregation towards degradable amorphous species.
This approach presents a versatile platform for Alzheimer's disease therapeutic exploration.