Laboratory of Biostructures

BIO1Engineering protein molecules that self-assemble into complex bioarchitectures is an innovative goal of nanobiotechnology. We aim to generate novel bioinspired protein scaffolds that can self-assemble upon stimulation into desired well-ordered and stable multicomponent nanobiostructures, such as biomolecular cages and biocrystals. This process is strongly driven by specific technological needs. Applications can range from design of bioactive 3D nanobiomaterials and nanobiosensors, to designed biomedicines. My research interests also focus on the relationships biostructure/interactions/function of innovative membrane protein targets relevant for metabolic and neurological disorders, and the discovery of privileged chemicals as leads to novel drugs.

Primary research tools include approaches of protein engineering, recombinant protein overexpression in mammalian and bacterial cell systems, production scale-up, biocrystallization, and structural biophysics analyses (mainly x-ray crystallography, single particle cryo-electron microscopy, small angle x-ray scattering and neutron scattering, surface plasmon resonance and isothermal titration calorimetry, supported by computational approaches). Overall, these methods provide insights into protein structure and dynamics at the atomic level, and allow us to characterize the thermodynamics and kinetics of protein interactions. Findings result in key parameters for efficient protein architecture design, and discovery of novel target modulators and drug leads.

The group of BIOSTRUCTURES has equipped laboratories of biochemistry, biophysics and cell biology, for the production and purification of proteins, their crystallization and characterization. We use highly sensitive, high-throughput and label-free techniques to study non-covalent biomolecular interactions, including surface plasmon resonance (SPR SensìQ Pioneer) and isothermal titration calorimetry (Microcal Auto-ITC200). The lab is supported by a facility of mass spectrometry and peptide solid-phase synthesis. We have access to major European Synchrotron Radiation Facilities, including ESRF (Grenoble), DIAMOND (Oxford) and ELETTRA (Trieste).


Group Members


  • Gianpiero Garau 
  • Eleonora Margheritis 
  • Valentina De Lorenzi 
  • Sara Chiarugi 
  • Aurora Russo 
 BIO Page Image Group



  • Gabriel A Frank, Ben-Gurion University of the Negev, Israel.
  • Alexander Dityatev, DZNE - Center for Neurodegenerative Diseases, Germany.
  • Antimo Gioiello, University of Perugia, Italy.
  • Simona Rapposelli, University of Pisa, Italy.
  • Dr Ranieri Bizzarri & Riccardo Nifosì, CNR-Nano - Scuola Normale Superiore, Pisa, Italy.


  • Bile Acid Recognition by NAPE-PLD.     

Margheritis E, Castellani B, Magotti P, Peruzzi S, Romeo E, Natali F, Mostarda S, Gioiello A, Piomelli D, Garau G*

2016 ACS Chemical Biology 11:2908-2914.

  • Facile fabrication of bioactive ultra-small protein-hydroxyapatite nanoconjugates via liquid-phase laser ablation and their enhanced osteogenic differentiation activity

Rodio M, Coluccino L, Romeo E, Genovese A, Diaspro A, Garau G*, Intartaglia R

2016 Journal of Matererial Chemistry B. 

  • Heparin/heparan sulfates bind to and modulate neuronal L-type (Cav1.2) voltage-dependent Ca2+ channels.
Garau G, Magotti P, Heine M, Korotchenko S, Lievens PM, Berezin V, Dityatev A 2015
Experimental Neurology 274: 156-165.
  • Structure of human NAPE-PLD: regulation of fatty acid ethanolamide biosynthesis by bile acids.
Magotti P, Bauer I, Igarashi M, Babagoli M, Marotta R, Piomelli D, Garau G*
2015 Structure (Cell) 23:598-604.
  • A Binding Site for Nonsteroidal Anti-inflammatory Drugs in Fatty Acid Amide Hydrolase.
Bertolacci L, Romeo E, Veronesi M, Magotti P, Albani C, Dionisi M, Lambruschini C, Scarpelli R, Cavalli A, De Vivo M, Piomelli D, Garau G*
2013 Journal of the American Chemical Society 135:22-25.


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