Cell Membrane Properties can Mediate the Toxicity of Protein Misfolded Oligomers and Folded Toxins

The onset and progression of Alzheimer's disease is characterized by the aggregation 42-residue form amyloid-β peptide (Aβ42). Significant evidence indicates that mechanism which Aβ42 induces cell death through interaction its toxic oligomeric species with membranes, results in disruption membrane integrity homeostatic processes within cell. Moreover, there interacts differentially regions membranes enriched different components, cytotoxicity increased as size oligomers decreases their hydrophobicity increases. We investigate influence composition, coupled these biophysical parameters, on ability to induce cellular dysfunction order better understand deleteriously interact neuronal cells. By modifying composition SH-SY5Y human neuroblastoma cells using small molecules measuring response oligomers, we identify components impact cytotoxic effects oligomers. also measure modified folded biotoxins an analogous fashion Aβ42, providing a general view how properties behavior biomolecules. Our illustrate importance toxins suggest possible therapeutic targets for protection from agents common mechanism.