Universally conserved molecular chaperone machines assist de novo protein folding and efficiently rescue cellular proteins from cytotoxic aggregation induced by stress, aging or certain mutations. Alzheimer's disease is the most frequent type of dementia and to date there is no early diagnosis technic or curative treatment available. Alzheimer is directly linked to protein aggregation and it has been proposed that the use of molecular chaperones might lead to promising new therapeutic approaches. In this work, we have looked upon a bacterial chaperone with an unusually robust holdase activity, as a promising modulator of Alzheimer's related Amyloid Beta (AB) peptide aggregation.