Finally, the potential role of C 60 A molecules on CTPR8Y 16 aggregation was explored. To this end, five replicas of 200 ns of MD simulations were carried out with 24 C 60 A molecules and three CTPR8Y 16 protein units. The simulations showed that fullerene molecules first aggregate and then contribute to the formation of CTPR8Y 16 aggregates, acting as bridge molecules between CTPR8Y 16 units (Fig. ). Despite the short simulation time of these simulations and the model system used, MD simulations revealed a direct contribution of C 60 A to the formation of CTPR8Y 16 assemblies. The simulated behaviour of fullerenes is consistent with experimental observations, as free C 60 A fullerenes aggregate in aqueous solution to form thin amorphous filaments (Fig. ). These filaments, however, have no uniform structure and produce no electron diffraction; the assembly is thus likely governed by non-specific interactions observed in the simulations. The contacts with the ordered surface of CTPR protein, however, seem to serve as nucleation points for crystalline-ordered fullerene assemblies. Reciprocally, the fullerenes appear to mediate and strengthen the interactions between the proteins that normally manifest in protein assemblies in solid state.