The aggregation of the Amyloid beta 1-40 (Aβ1-40) coated nano-particles involves a networking between Aβ1-40 at nano-scale interface. While the details of peptide conformation at the nano-scale interface has not been known, the aggregation was known to be initiated by the unfolded Aβ1-40 monomers. An empirical peptide coverage ratio was extracted for 20 nm gold colloid and 50 nm gold colloid to be approximately 0.75 and 0.45, respectively. By adding the Aβ1-40 to the 20 nm and 50 nm gold colloidal particles, different gold colloid aggregates formation paths were identified. For the 20 nm gold colloid particle, it had two different induction points (i.e., two step-function responses) for gold’s aggregation. On the contrary, there was only one moderate induction point for the aggregation of 50 nm gold colloid particles. The aggregation model based on stepwise coverage ratio is proposed to explain the difference in aggregation formation mechanism between 20 nm and 50 nm gold colloid.

Investigation of the aggregates formation mechanism of Amyloid beta 1-40 coated nano-gold particles

2019 Fall National Meeting

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