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On the other hand, regular physical exercise is known to significantly reduce the risk of developing AD. Here, it is reported on the transformation and toxicity mitigation of A\u03b2 amyloid aggregation by a spontaneous \u201ccorona\u201d of \u03b2\u2010endorphin, a major peptide hormone released upon exercise to suppress post\u2010exercise pain. Given that both A\u03b2 and \u03b2\u2010endorphin co\u2010localize extracellularly in the brain, it is postulated that \u03b2\u2010endorphin may mitigate the toxicity of A\u03b2 aggregation via direct molecular interactions, thereby contributing to an exercise\u2010mediated reduction of AD risk. Combining biophysical characterizations in vitro with atomistic discrete molecular dynamics simulations in silico, a strong interaction is shown between \u03b2\u2010endorphin and A\u03b2, where \u03b2\u2010endorphins are located at the periphery to render a corona of their hetero\u2010complexes with A\u03b2. 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