This research focuses on a folding or unfolding process of amyloidogenic peptides, amyloid beta, alpha synuclein and beta-2 microglobulin under an interfacial environment. We use an approach to provide surface potential required for a folding through nanogold colloidal particles.  The folded or unfolded conformation of peptides can be prepared by externally changing the pH to pH10 or pH4, respectively. Corresponding the folded or unfolded conformation of the peptides pre-adsorbed over the gold particles create either dispersed or aggregated condition of gold particles, resulting in a no-shift or red-shift of SPR (Surface Plasmon Resonance) band for various sizes of gold colloids.  Generally speaking, the enhancement of the reversible self-assembly depend on the size of nano-gold colloid. The temperature- dependence of the reversibility exhibited a complex feature. Mostly, the enhancement took place at the relatively higher temperature. However, the opposite trends were observed depending on the peptide studied.<br/>

Nano-scale interfacial reversible protein folding of amyloidogenic peptides

256th National Meeting (2018)

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