RESUMO
BACKGROUND: Beta-amyloid peptide (Aß) is the key protein in the pathogenesis of Alzheimer's disease, the most common age-related neurodegenerative disorder in humans. Aß peptide induced pathological phenotypes in different model organisms include neurodegeneration and lifespan decrease. However, recent experimental evidence suggests that Aß may utilize oligomerization and fibrillization to function as an antimicrobial peptide (AMP), and protect the host from infections. We used the power of Drosophila model to study mechanisms underlying a dual role for Aß peptides. RESULTS: We investigated the effects of Drosophila treatment with three Aß42 peptide isoforms, which differ in their ability to form oligomers and aggregates on the lifespan, locomotor activity and AMP genes expression. Aß42 slightly decreased female's median lifespan (by 4.5%), but the effect was not related to the toxicity of peptide isoform. The lifespan and relative levels of AMP gene expression in male flies as well as locomotor activity in both sexes were largely unaffected by Aß42 peptide treatment. Regardless of the effects on lifespan, Aß42 peptide treatment induced decrease in AMP genes expression in females, but the effects were not robust. CONCLUSIONS: The results demonstrate that chronic treatment with Aß42 peptides does not drastically affect fly aging or immunity.