Submission Type
Poster
Abstract
Alzheimer’s Disease (AD) is a neurological disorder characterized by a buildup of the amyloid beta (Aβ) peptide as aggregate species in the brain. Recent advances using antibody based treatments which target Aβ have seen clinical success, achieving FDA approval. However, they come at a significant cost, ranging from $20,000-40,000 a year. Ruthenium-based therapeutics are promising alternatives, as they have shown an ability to modulate the aggregation of Aβ in solution and prevent its cytotoxicity. Despite their initial success, significant questions regarding the affinity of the complexes for Aβ relative to endogenous proteins remain unknown. Therefore, we have synthesized a series of phenanthroline ruthenium-based complexes and assessed their respective ability to modulate Aβ aggregation while also evaluating their association with the serum protein albumin (HSA). The impact on Aβ aggregation for the complexes was assessed using thioflavin T fluorescence, dynamic light scattering, and transmission electron microscopy. Alternatively, the affinity of the complexes for HSA was determined using fluorescence binding assays. The results of these experiments will be discussed, where structure-activity relationships will be established.
Recommended Citation
Loughlin, Maria; Grabowski, Emma; Hacker, Ryan; and Smith, Jacob, "233 - Synthesis and Evaluation of 1,10-Phenanthroline Ruthenium-Arene Complexes to Modulate the Aggregation of the Amyloid-β Peptide" (2025). GREAT Day Posters. 72.
https://knightscholar.geneseo.edu/great-day-symposium/great-day-2025/posters-2025/72
233 - Synthesis and Evaluation of 1,10-Phenanthroline Ruthenium-Arene Complexes to Modulate the Aggregation of the Amyloid-β Peptide
Alzheimer’s Disease (AD) is a neurological disorder characterized by a buildup of the amyloid beta (Aβ) peptide as aggregate species in the brain. Recent advances using antibody based treatments which target Aβ have seen clinical success, achieving FDA approval. However, they come at a significant cost, ranging from $20,000-40,000 a year. Ruthenium-based therapeutics are promising alternatives, as they have shown an ability to modulate the aggregation of Aβ in solution and prevent its cytotoxicity. Despite their initial success, significant questions regarding the affinity of the complexes for Aβ relative to endogenous proteins remain unknown. Therefore, we have synthesized a series of phenanthroline ruthenium-based complexes and assessed their respective ability to modulate Aβ aggregation while also evaluating their association with the serum protein albumin (HSA). The impact on Aβ aggregation for the complexes was assessed using thioflavin T fluorescence, dynamic light scattering, and transmission electron microscopy. Alternatively, the affinity of the complexes for HSA was determined using fluorescence binding assays. The results of these experiments will be discussed, where structure-activity relationships will be established.
Comments
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