Biochemistry and Molecular Biophysics. Coordinator: Francia

The research activity is aimed at understanding the membrane/protein-solvent interaction at the molecular level and at characterizing glassy disaccharide and protein matrices with biopreservative properties.

Research themes

Use of bioenergetically active membranes for the study of eco-compatible solvents 

The use of eco-compatible substances is the primary objective of green chemistry. Among these, ecocompatible solvents and surfactants (ionic liquids, eutectic solvents) and biobased chemicals play a central role. The interaction of these compounds with biological entities and their environmental impact vary considerably and show a high species-specificity. The laboratory studies the effects of substances considered green on the integrity of native biological membranes isolated from photosynthetic bacteria and mitochondria, and their effects on the growth of microorganisms in culture. The use of bioenergetically active biological membranes, isolated in vesicular form, offers the advantage of deepening the mechanism of action of exogenous molecules, allowing us to distinguish between direct inhibition on one or more of the complexes responsible for energy transduction and indirect inhibition, due to the uncoupling of the proton-motive force from ATP synthesis. 

Bioprotection mechanisms in dehydrated glassy matrices 

The insertion of biomolecules, in particular proteins, into sufficiently dehydrated glassy matrices of the disaccharides trehalose and sucrose produces a drastic inhibition of the conformational dynamics of the biomolecule on a large time scale, resulting in an exceptional thermal stability. This behavior is the basis of the natural phenomenon of anhydrobiosis and of numerous applications in the pharmaceutical and biotechnological fields. Our group, in collaboration with L. Cordone (Department of Physics and Astronomy, University of Palermo), has formulated a molecular model of bioprotection (anchorage hypothesis) which leads the dynamic protein-matrix coupling to the formation of extensive H bond networks to protein surface groups, residual water molecules and disaccharides. To verify the model and define its molecular details, we characterize the structure and dynamics of amorphous matrices formed by model proteins and disaccharides (or other co-solutes synthesized under stress conditions by anhydrobiotic organisms) by static FTIR spectroscopy. Recently these studies have been extended to the characterization of the bioprotective properties of dehydrated matrices consisting of intrinsically disordered proteins (CAHS), purified from anhydrobiotic organisms. 

Lab Members

Francesco Francia,  Associate Professor (e-mail)

Giovanni Venturoli,  Alma Mater Professor (e-mail)

Tancredi Bin, PhD Student

Internship projects

Internship pojects focused on the research themes summarized above are available for First cycle degree (Corso di Laurea in Scienze Biologiche, Corso di laurea in Biotecnologia) and Second cycle degree (Corso di laurea Magistrale in Biologia Molecolare e Cellulare, Biotecnologie Molecolari e Industriali).

Main publications

  • Bin,T., Venturoli,G.,  Ghelli,A.M., Francia,F. (2024) "Use of bacterial photosynthetic vesicles to evaluate the effect of ionic liquids on the permeability of biological membranes", Biochim. Biophys. Acta - Biomembranes, 1866: 184291.
  • Mamedov,M.D., Milanovsky,G.E., Malferrari,M., Vitukhnovskaya,L.A., Francia,F., Semenov,A.Y., Venturoli,G. (2021). “Trehalose matrix effects on electron transfer in Mn-depleted protein-pigment complexes of Photosystem II.” BBActa 1862: 1484413.

  • Malferrari, M., Francia, F. and Venturoli, G. (2015). “Retardation of protein dynamics by trehalose in dehydrated systems of photosynthetic reaction centers. Insights from electron transfer and thermal denaturation kinetics.” J. Phys. Chem. B 119: 13600-13618.

  • Malferrari,M., Malferrari,D., Francia,F., Galletti,P., Tagliavini,E., Venturoli,G. (2015). “Ionic liquids effects on the permeability of photosynthetic membranes probed by the electrochromic shift of endogenous carotenoids.” BBActa 1848: 2898-2909.

  • Francia, F., Dezi, M., Mallardi, A., Palazzo, G., Cordone, L. and Venturoli, G. (2008) “Protein-matrix coupling/uncoupling in “dry” systems of photosynthetic reaction center embedded in trehalose/sucrose: the origin of trehalose peculiarity.” J. Am. Chem. Soc. 130: 10240-10246.