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The pathological process of Alzheimer's disease is closely related to amyloid fibril formation by the causative protein, amyloid  (A). The growth behavior of A fibrils is predominated by the seeds-monomeric A interaction. In this study, the local hydrophobicity of seeds of A fibrils was investigated by the aqueous two-phase partitioning method to evaluate the hydrophobic interaction between the seed-monomeric A. The seeds showed a high local hydrophobicity relative to the monomer and fibrils. From the fibril growth experiment and the additive effect of Triton X-100, we could demonstrate the contribution of the hydrophobic seeds-monomer interaction to fibril formation.

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