Abstract
The ability of nanoparticles to influence protein folding and aggregation is interesting, not only because of the potential beneficial applications, but also the potential risks to human health and the environment. The interactions of concanavalin A (Con A) with zinc oxide nanoparticles (ZnO-NPs) were investigated by using fluorescence, fourier transform infrared spectroscopy, circular dichroism (CD) and dynamic light scattering techniques. ANS fluorescence and CD spectroscopy authenticated the formation of molten globule state of Con A after its incubation with ZnO-NPs for 36 h. Further incubation of 48 h resulted in the aggregation of unadsorbed Con A, proved by decrease in ANS fluorescence while an increase in thioflavin T fluorescence, characteristic of an aggregates. Moreover, Fourier transform-infrared spectroscopy confirmed the aggregation of unadsorbed Con A. The aggregated products were negligible genotoxic as analyzed by pUC19 plasmid degradation and comet assay. It is clear that ZnO-NPs morphology affect unadsorbed proteins structure. A better understanding of these differences will be essential to engineer fully functional nanobioconjugates and NPs which do not damage the proteins present in the biological system.