Alzheimer's disease and inclusion body myositis (IBM) are disorders frequently found in the elderly and characterized by the presence of amyloid-β peptide (Aβ) aggregates. We used Caenorhabditis elegans that express Aβ in muscle cells as a model of IBM, with the aim of analyzing Aβ-induced muscle pathology and evaluating the consequences of modulating Aβ aggregation. First, we tested whether the altered motility we observed in the Aβ transgenic strain could be the result of a compromised neuromuscular synapse. Our pharmacological analyses show that synaptic transmission is defective in our model and suggest a specific defect on nicotine-sensitive acetylcholine receptors (AChRs). Through GFP-coupled protein visualization, we found that synaptic dysfunction correlates with mislocalization of ACR-16, the AChR subunit essential for nicotine-triggered currents. Histological and biochemical analysis allowed us to determine that copper treatment increases the amyloid deposits and decreases Aβ oligomers in this model. Furthermore, copper treatment improves motility, ACR-16 localization, and synaptic function and delays Aβ-induced paralysis. Our results indicate that copper modulates Aβ-induced pathology and suggest that Aβ oligomers are triggering neuromuscular dysfunction. Our findings emphasize the importance of neuromuscular synaptic dysfunction and the relevance of modulating the amyloidogenic component as an alternative therapeutic approach for this debilitating disease.