The amyloid beta peptide 1-40 (Aβ1-40) was prepared over nanogold colloidal surfaces together with Thioflavin T (ThT)dye as a fluorophore as Aβ1-40 proceeds a folding conformational change. A series of studies on fluorescence decay time were analyzed at pH’s (pH 1 – 12), and with gold colloidal sizes ranging from 10 nm to 100 nm. It was speculated that ThT attached to either 22Glu or 23Asp of the Aβ1-40 through an electrostatic interaction between adjacent Aβ1-40 monomers. The spacing between adjacent Aβ1-40 monomers must be increased for gold colloidal sizes of 50 nm and above. We attempted to extract the ThT attachment site in Aβ1-40, and it was speculated that the hydrophilic segment of Aβ1-40 was used in binding to the gold colloidal surface and hydrophilic site of Aβ1-40, networking with the other Aβ1-40 adsorbed on the gold colloidal surface. This study provided a significant evidence supporting that Aβ1-40 has higher binding affinity than a gold colloidal surface.

Investigation of nanoscale interfacial interaction of amyloid beta peptide

256th National Meeting (2018)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.