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Inhibition of Amyloid Aggregates in C. Elegans as a Model for Treatment of Alzheimer’s and Parkinson’s Disease

Parkinson’s Disease (PD) and Alzheimer’s Disease (AD) are neurodegenerative diseases characterized by pathogenic amyloid aggregates that lead to loss of brain function, which globally affect more than 10 million1 and 44 million2 patients, respectively. PD is prevalent in 1% of adults over the age of 601 while 1 in 9 adults over 65 are diagnosed with AD3. Currently, these diseases cannot be cured and are therefore of high interest to scientists. This study utilizes three strains of Caenorhabditis elegans, a transparent nematode, as a model for the treatment of these pathologies. The GMC101 strain of genetically modified C. elegans overexpresses A-β 1-42 peptide in muscle cells. These peptides form amyloid aggregates over time associated with the onset and progression of AD in humans. Another strain, NL5901, overexpresses α-Synuclein peptide, leading to the aggregation of these amyloid peptides linked to PD in humans. This study applies small molecules to inhibit amyloid aggregation to slow or stop the progression of these diseases. The effectiveness of treatment is measured via 14-days motility assays of C. elegans strains with treatment, strains without treatment, and wild-type N2 strain serving as control. Results show that the FDA-approved anticancer drug Bexarotene inhibits A-β 1-42 peptide aggregation in GMC101 strains of C. elegans while the molecule SK129, synthesized by Principal Investigator Dr. Sunil Kumar, inhibits α-Synuclein peptide aggregation in the NL5901 strains of C. elegans. These data suggested that future application of these treatments in human patients could hinder the development of these amyloid-related pathologies.

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