The fluorescein attached to Amyloid beta 1-40 ( FAb)  was utilized to investigate a hydrophilic-charge interaction at the nano-scale interface of gold nano-particle under Dimethyl-sulfoxide (DMSO) environment. As FAb interacted with various sizes of gold nano-colloidal particles ranging in size between 10 nm and 100 nm in diameter, the research team observed the intensive quenching of the fluorescence. The research team hypothesized that the FAb adsorbed over the nano-colloidal surface through the hydrophilic (N-terminal side) segments. The entire dynamical profile of fluorescein can be understood as a relative degree of interaction between a fluorescein and the gold nano-particle surface. Therefore, fluorescence quenching features must imply that fluorescein attached side (C-terminal) is closely located to the nano-gold colloidal surface.

Fluorescence quenching mechanism by the interaction of amyloid beta peptide and nano-gold particle

2019 Fall National Meeting

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