Abstract
Amyloid-β (Aβ) peptide Aβ19–20 tends to self-assemble into well-ordered tubular structures under physiological conditions, while in the presence of equimolar Cu(II), they assembled into homogeneous microvesicles; a chelator can competitively bind to Cu(II) from the Cu(II)–Aβ19–20 complex, resulting in reforming of the peptide tubular structure.
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