Chaperon-Mediated single molecular approach toward modulating aβ peptide aggregation

We report here a single molecular approach using chaperone-like molecular modulators for modulating the aggregation behavior of a vital analogue of beta-amyloid peptide (Aβ) by using scanning tunneling microscopy. The molecular structures of the β-sheets for Aβ33-42 peptide are revealed, which are keen to the aggregation of Aβ42 relating to Alzheimer's disease. It was identified that the introduction of chaperonelike modulators could regulate the assembling behavior of the peptide at molecular level. Furthermore, the modulators could also significantly accelerate the aggregation of the peptide in aqueous solution as revealed by light scattering studies. These observations of the molecular modulator effect in peptide assemblies could provide a novel approach toward modulating Aβ peptide aggregations.