The folding process of the amyloidogenic peptide is regarded as the crucial conformational change leading to fibrillogenesis, which eventually triggers neurodegenerative diseases. Our recent studies indicate that a key oligomeric form associated with fibrillogenesis can be stably made provided by a metal surface potential. In recent studies, we successfully identified the layer of Beta-2-Microglobulin (β2M) to be approximately 0.9 nm in width over a 30 nm gold colloid surface. This layer is used to aggregate residual β2M coated gold colloid particles under only acidic conditions, in which unfolded β2M oligomers were formed. While we are not certain if this layer is a monolayer or multilayer, the oligomeric form can determine this thickness. Therefore, the layer’s thickness showed signs of being dependent on the size of the gold colloid. We are investigating the stable form of the oligomer and associated layer’s thickness over the gold colloidal size between 10 nm and 100 nm, as well as a pH ranging from 2-12.

Investigation of reversible self-assembly of amyloidogenic peptides at nano-scale interface

253rd National Meeting (2017)

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