Abstract

Negatively charged gold nanoparticles featuring 2-(10-mercapto-decyl)-malonic acid were synthesized using the Murray place-displacement reaction. These water-soluble malonate gold mixed monolayer protected clusters (MMPCs) effectively bind and inhibit chymotrypsin based on complementary electrostatic surface recognition. The effect of increasing ionic strength on inhibition was also studied. It was observed that addition of high ionic strength solutions to protein-nanoparticle complexes show almost complete restoration of protein activity. The conformational change of chymotrypsin upon binding to the MMPC was investigated using fluorescence spectrometry and circular dichroism, thus correlating structural changes with enzyme activity.

Keywords: protein-protein interactions, mixed monolayer protected clusters, brust-schiffrin reduction, mercaptoundecanoic acid, circular dichroism, fluorescence spectroscopy, malonic acid