Submission Type

Poster

Abstract

The gold colloid coated with Aβ1-40 was characterized by using the Raman imaging technique. Through the observed pH-dependent shift of the SPR (Surface Plasmon Radiance) band, it was determined that gold colloid aggregates were formed under acidic conditions.. Remarkably, Aβ1-40 coated 20 nm gold supported quasi-reversible self-assembly of the aggregates as the pH was alternated between pH 4 and pH 10. The morphology was distinctly observable between two different conditions. Nevertheless, the SERS (Surface Enhanced Raman Scattering) spectrum presented minor differences. An additional analysis displayed the contrast in spectral density in the regions of 250 cm-1 and 1750 cm-1. The mode analysis distinguished in the reversible aggregation, the formation of aggregates with the important influence of the benzene ring components of Tyrosine and Phenylalanine. The disassembling of the aggregates, however, was intensified through the participation of Histidine, Glutamine, Methionine, and Aspartic acid.

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Sponsored by Kazushige Yokoyama

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236 - Characterization of Reversible Aggregation of Amyloid beta 1-40 Coated Gold Nano-Particles

The gold colloid coated with Aβ1-40 was characterized by using the Raman imaging technique. Through the observed pH-dependent shift of the SPR (Surface Plasmon Radiance) band, it was determined that gold colloid aggregates were formed under acidic conditions.. Remarkably, Aβ1-40 coated 20 nm gold supported quasi-reversible self-assembly of the aggregates as the pH was alternated between pH 4 and pH 10. The morphology was distinctly observable between two different conditions. Nevertheless, the SERS (Surface Enhanced Raman Scattering) spectrum presented minor differences. An additional analysis displayed the contrast in spectral density in the regions of 250 cm-1 and 1750 cm-1. The mode analysis distinguished in the reversible aggregation, the formation of aggregates with the important influence of the benzene ring components of Tyrosine and Phenylalanine. The disassembling of the aggregates, however, was intensified through the participation of Histidine, Glutamine, Methionine, and Aspartic acid.

 

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