CTPR proteins were identified as good candidates for hosting fullerenes due to high abundance of tyrosine (6 residues per repeat), that could form - stacking interactions with the fullerenes (Fig. ). Protein composed of eight repeats comprising a full superhelical turn, CTPR8, was chosen as the scaffold, given the stability and the well characterised properties of the eight-repeat protein. In addition to the shape compatibility to accommodate carbon nanoforms in the hydrophobic inner cavity, 13 the CTPR protein also contains inward-pointing lysine residues that can further stabilise the protein-C 60 conjugates.