By utilizing of enhanced Thioflavin�T (ThT) fluorescence upon binding proteins, we investigate the spectra in an attempt to correlate conformational change (folded or unfolded) over the nanocolloidal surface under various concentrations as well as pHs. The fluorescence intensity was found to increase as concentration of amyloid beta or ovalbumin was increased.  Our results provided an evidence of an enhancement of fluorescence prominently in pH 9-pH10. When we tested for a reversibility in observed fluorescence with respect to an external pH fluctuations between pH 4 and pH10, there was a slight sign of reversibility only when 20 nm gold colloid was present.  We conclude that fluorescence data can potentially be utilized to correlate the protein conformation over the gold nanocolloidal surface.

Fluorescence study probing the conformational change of protein adsorbed on the nanocolloidal surface

248th National Meeting (2014)

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