Stabilization of lysozyme in aqueous dispersion of graphene oxide sheets

This study examines the effect of surface oxygen groups upon ability of graphene oxide (GO) sheets in sup-pressing the fibrillation of lysozyme (LYZ). Graphite was oxidized using 6 and 8 wt equivalents of KMnO4, and as produced sheets were abbreviated as GO-06 and GO-08, respectively. Particulate characteristics of sheets were characterized by light scattering and electron microscopic techniques, and their interaction with LYZ was ana-lysed by circular dichroism (CD) spectroscopy. After ascertaining acid-driven conversion of LYZ to fibrillary form, we have shown that the fibrillation of dispersed protein can be prevented by adding GO sheets. Inhibitory effect could be attributed to binding of LYZ over the sheets via noncovalent forces. A comparison between GO-06 and GO-08 samples showed superior binding affinity of the latter. Higher aqueous dispersibility and density of oxygenated groups in GO-08 sheets would have facilitated the adsorption of protein molecules, thus making them unavailable for aggregation. Pre-treatment of GO sheets with Pluronic 103 (P103, a nonionic triblock copolymer), caused reduction in the adsorption of LYZ. P103 aggregates would have rendered the sheet surface unavailable for the adsorption of LYZ. Based on these observations, we conclude that fibrillation of LYZ can be prevented in association with graphene oxide sheets.

Automated summary

This study investigates the impact of surface oxygen groups on the ability of graphene oxide (GO) sheets to suppress the fibrillation of lysozyme (LYZ). GO sheets were produced by oxidizing graphite with different amounts of KMnO4. The particulate characteristics of the sheets were analyzed, and their interaction with LYZ was examined using circular dichroism spectroscopy. The results showed that the fibrillation of dispersed protein can be prevented by adding GO sheets, and the inhibitory effect is attributed to the binding of LYZ to the sheets via noncovalent forces.