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Alzheimer’s disease (AD) is one of the most common age-associated pathologies, which inevitably leads to dementia and death. The aggregation of β-amyloid (Aβ) peptides on plaques in brain tissue is strongly associated with AD. The possible link between aluminum and AD still remains controversial. In this work, the aggregation of Aβ40 induced by Al(III) was investigated with the use of the fluorescence quenching method, UV–visible and circular dichroism spectroscopies as well as the atomic force microscopy technique. The results demonstrated that Al(III) induced the transformation of the initial random coil structure to the β-sheet configuration in the Aβ40 peptides. These structural changes facilitated the aggregation of Aβ40. Also, the binding constant was calculated with the use of the multivariate curve resolution-alternating least squares (MCR-ALS) chemometrics method. Keywords: Alzheimer’s disease, β-Amyloid peptides, Spectroscopy, Chemometrics