Enhanced activity of chaperonin GroEL in the presence of platinum nanoparticles

Abstract

The chaperonin protein GroEL was mixed with varying concentrations of K2PtCl4 followed by a 20-fold concentration of sodium borohydride to afford GroEL–platinum nanoparticle complexes in a ratio of between 1:25 and 1:2,000. Typical colour change, from colourless or pale yellow to brown, occurred that was dependent on the amount of platinum present. These complexes were characterised by UV/Vis, inductively coupled plasma optical emission spectroscopy, Fourier transform infra red, transmission electron microscopy (TEM) and energy dispersive X-ray spectroscopy. TEM analysis revealed that the size of nanoparticles increased as the molar ratio of platinum to GroEL increased with an average size diameter of 1.72–3.5 nm generated with GroEL–platinum molar ratios of 1:125–1:2,000. Fourier-transform infrared spectroscopy (FTIR) spectra showed no distinct changes in the structure of GroEL but confirmed that the nanoparticles were attached to the protein. The effect of platinum nanoparticles on the ATPase activity of GroEL showed an activity of 5.60 μmol min−1 ml−1 (87 % increase over a control) at the molar ratio of GroEL–platinum nanoparticles of 1:25.