Despite the advances in understanding of protein manipulation and creation of artificial constructions with enhanced properties, rational protein design is still far from straightforward due to the limited understanding of the sequence-structure-function relationship. The problem is somewhat mitigated when working with small repeat proteins, that are amenable to modular design and thus allow local modifications without affecting global structure. Consensus tetratricopeptide repeat (CTPR) protein has been particularly useful in the synthesis of hybrid materials. CTPR proteins are made of modules of 34 amino acids, folded into a helix-turnhelix motif; however, the fold is defined by only 8 conserved residues, thus allowing a lot of freedom for protein engineering. The modules generally appear repeated in tandem, from 2 to 20 repeats, generating a rigid right-handed superhelical structure 8 that is able to function as stable scaffold in both biological and laboratory settings. 11 Thus, CTPR proteins have been successfully used to build photoconductive and electroactive systems, combining covalent modification and non-covalent interactions, as well as stabilise fluorescent and electroactive clusters. In the current work, the CTPR proteins were engineered into scaffolds for C 60 fullerene assembly. Carbon nanoforms combined with biomimetic nanomaterials have driven the advancement in nanoscience, biochemistry and materials chemistry in the recent years. C 60 fullerene, since its discovery, has been of particular interest due to its unique chemical and physical properties. The hydrophobic nature of the carbon species allows the fullerene to form complexes with proteins, leading to biological activity. A systematic computational analysis suggested the fullerene cage is able to scan the protein surface and identify a suitable hydrophobic pocket to accommodate.