Proteins as supramolecular hosts for C60: A true solution of C60 in water

Matteo Di Giosia, Paul H.H. Bomans, Andrea Bottoni, Andrea Cantelli, Giuseppe Falini, Paola Franchi, Giuseppe Guarracino, Heiner Friedrich, Marco Lucarini, Francesco Paolucci, Stefania Rapino, Nico A.J.M. Sommerdijk, Alice Soldà, Francesco Valle, Francesco Zerbetto, Matteo Calvaresi (Corresponding author)

Research output: Contribution to journalArticleAcademicpeer-review

32 Citations (Scopus)


Hybrid systems have great potential for a wide range of applications in chemistry, physics and materials science. Conjugation of a biosystem to a molecular material can tune the properties of the components or give rise to new properties. As a workhorse, here we take a C60@lysozyme hybrid. We show that lysozyme recognizes and disperses fullerene in water. AFM, cryo-TEM and high resolution X-ray powder diffraction show that the C60 dispersion is monomolecular. The adduct is biocompatible, stable in physiological and technologically-relevant environments, and easy to store. Hybridization with lysozyme preserves the electrochemical properties of C60. EPR spin-trapping experiments show that the C60@lysozyme hybrid produces ROS following both type I and type II mechanisms. Due to the shielding effect of proteins, the adduct generates significant amounts of 1O2 also in aqueous solution. In the case of type I mechanism, the protein residues provide electrons and the hybrid does not require addition of external electron donors. The preparation process and the properties of C60@lysozyme are general and can be expected to be similar to other C60@protein systems. It is envisaged that the properties of the C60@protein hybrids will pave the way for a host of applications in nanomedicine, nanotechnology, and photocatalysis.

Original languageEnglish
Pages (from-to)9908-9916
Number of pages9
Issue number21
Publication statusPublished - 7 Jun 2018


  • Fullerenes/chemistry
  • Muramidase/chemistry
  • Spin Trapping
  • Water/chemistry


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