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This study aims to elucidate the secondary nucleation process of A\u03b242 peptides by combining experimental and computational methods. Using a newly developed nanopipette\u2010based amyloid seeding and translocation assay, confocal fluorescence spectroscopy, and molecular dynamics simulations, the influence of the seed properties on A\u03b2 aggregation is investigated. Both fragmented and unfragmented seeds played distinct roles in the formation of oligomers, with fragmented seeds facilitating the formation of larger aggregates early in the incubation phase. The results show that secondary nucleation leads to the formation of oligomers of various sizes and structures as well as larger fibrils structured in \u03b2\u2010sheets. 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