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Gianpiero Garau

Group Leader - BIOSTRUCTUREs Lab

Research Line

Electron Crystallography




+39 050 509379
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Center for Nanotechnology Innovation@NEST - Scuola Normale Superiore, Pisa

Department of Drug Discovery - ISTITUTO ITALIANO DI TECNOLOGIA (IIT)



The research in my lab aims to engineer and generate novel bioinspired protein scaffolds that can self-assemble upon stimulation into desired well-ordered and stable multicomponent nano-biostructures. This process is strongly driven by specific technological needs. Engineering protein molecules that self-assemble into desired complex bioarchitectures is an exciting prospect of nanobiotechnology. Applications can range from design of bioactive 3D nanobiomaterials to cascade biocatalysis in sustainable technology, from bioelectronics to biomolecular medicine. 
Our research interests also focus on the structure | function | interactions of innovative membrane protein targets, relevant for metabolic disorders and inflammation, and the discovery of privileged chemical structures as leads to novel drugs.

Primary research tools include approaches of structural biophysics and biotechnology. Among these, we use maily protein design & engineering, directed enzyme evolution, x-ray diffraction & electron crystallography, single particle cryo-electron microscopy, mass spectrometry, surface plasmon resonance, microcalorimetry, supported by advanced computational methods.

Gianpiero Garau (P.I.)
Eleonora Margheritis (postdoc)
Valentina De Lorenzi (postdoc),
Sara Chiarugi (PhD fellow)
Elisa Martino (PhD fellow)



=> If you are a highly motivated young postdoc / PhD candidate and aim to join us, please do not hesitate to contact me.




Structural Biophysics Protein Engineering Biotechnology Biomaterials Biointeractions Biocatalysis Ligand Discovery & Design




> BioStructure Design

With this project we aim to generate novel bioinspired protein scaffolds that can self-assemble upon stimulation into desired well-ordered and stable multicomponent nanobiostructures for specific technological needs.

This project is supported by grant funding from the CANON RESEARCH FOUNDATION IN EUROPE.


 biocages_2.jpg  GARAU_GIANPIERO_Journal Cover_IUCrJ_1.jpg GARAU_GIANPIERO_Canon1.jpg





> NAPE-PLD Interactions in Metabolic Diseases

The membrane-associated enzyme NAPE-PLD generates bioactive lipid amides that play important roles in stress and pain response, appetite and lifespan. Our studies have shown the molecular mechanism of their biogenesis and unveiled that the natural bile acids drive it. This discovery brings together bile acid physiology and lipid amide signaling, linking major players in lipid homeostasis with major players in lipid signaling. Small-molecule modulators of NAPE-PLD can have application in several metabolic and inflammatory disorders.

This project is carried out with financial support from the Italian Ministery of Foreign Affairs and Internation Cooperation (MAECI) [ ] ( Italy-Israel Joint Innovation Program for Industrial, Scientific and Technological Cooperation in R&D, Project SBD2-CNI-BGU ), and the European Commission (FP7 Project N. 268385) [ ].


 Cover_ACS CHEM Biol_2016.jpg


  • CHEMICAL BIOLOGY (ACS): Bile Acid Recognition and Lipid Amide Signaling


  • STRUCTURE (Cell Press): Structure of human NAPE-PLD 


  • CHEMISTRY & BIOLOGY (Cell Press): Bile Acids as Enzyme Regulators

  • SYNCHROTRON ELETTRA (Trieste, Italy): Crystal Structure of Human NAPE-PLD

  • FP7 COMMENTS: The secrets of anti-ageing

Longevity and healthy ageing are affected by our diet and lifestyle. EU-funded researchers have associated certain organic compounds called fatty acid ethanolamides (FAEs) with obesity and ageing


Selected Publications


  • Nanobeam precession-assisted 3D electron diffraction reveals a new HEWL polymorph
    Lanza A, Margheritis E, Mugnaioli E, Valentina C, Garau G, Gemmi M
    2019 IUCrJ  6:178-188. (+ Journal Cover)

    HIGHLIGHT: Why conferences matter - musings from crystallographic meeting. E.N. Baker
  • Role of Gln222 in photoswitching fluorescent proteins: a twisting and H-bonding affair?
    Storti B, Margheritis E, Abbandonato G, Domenichini G, Dreir J, Testa I, Garau G, Nifosì R, Bizzarri R
    2018 ACS Chemical Biology 13:2082-2093.
  • 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. (+ Journal Cover)
  • 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.
  • A catalytically silent FAAH-1 variant drives anandamide transport in neurons.
    Fu J, Bottegoni G, Sasso O, Bertorelli R, Rocchia W, Masetti M, Lodola A, Armirotti A, Garau G, Bandiera T, Reggiani A, Mor M, Cavalli A, Piomelli D
    2011 Nature Neuroscience 15:64-69.
  • Energy Landscapes Associated with Macromolecular Conformational Changes from Endpoint Structures.
    Fornili A, Giabbai B, Garau G, Degano M
    2010 Journal of the American Chemical Society 132:17570–17577.
  • Spectroscopic and structural study of proton and halide ion cooperative binding to gfp.
    Arosio D, Garau G, Ricci F, Marchetti L, Bizzarri R, Nifosì R, Beltram F
    2007 Biophysical Journal 93:232-244.
  • Structural basis for mammalian vitamin B12 transport by transcobalamin.
    Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L
    2006 Proceeding of the National Academy of Science USA. 103:4386-4391.
  • Structure-based phylogeny of the metallo-beta-lactamases.
    Garau G, Di Guilmi AM, Hall BG
    2005 Antimicrobial Agents and Chemotherapy 49: 2778-2784.
  • Crystal structure of phosphorylcholine esterase domain of the virulence factor choline-binding protein e from Streptococcus pneumoniae: new structural features among the metallo-beta-lactamase superfamily.
    Garau G, Lemaire D, Vernet T, Dideberg O, Di Guilmi AM
    2005 Journal of Biological Chemistry 280:28591-28600.
  • A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem.
    Garau G, Bebrone C, Anne C, Galleni M, Frère JM, Dideberg O
    2005 Journal of Molecular Biology 345:785-795.


BOOK: Beta-Lactamases. Ed. Jean-Marie Frère, Nova Publishers 2011.
X-ray structures and mechanisms of metallo-beta-lactamases.
Gianpiero Garau, Isabel Garcia-Saez, Laurent Chantalat, Andrea Carfi, Otto Dideberg.
Chapter 3, pp. 41-77.

HIGHLIGHTS: Synchrotron ELETTRA Research 2005-2006.
Wuerges J, Garau G, Geremia S, Randaccio L.
Crystal structure of human and bovine Vitamin B12-transport protein Trascobalamin.
Section Structural Biology, pp. 71-73.


Publications, Citations, H-index:






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I numeri di IIT

L’Istituto Italiano di Tecnologia (IIT) è una fondazione di diritto privato - cfr. determinazione Corte dei Conti 23/2015 “IIT è una fondazione da inquadrare fra gli organismi di diritto pubblico con la scelta di un modello di organizzazione di diritto privato per rispondere all’esigenza di assicurare procedure più snelle nella selezione non solo nell’ambito nazionale dei collaboratori, scienziati e ricercatori ”.

IIT è sotto la vigilanza del Ministero dell'Istruzione, dell'Università e della Ricerca e del Ministero dell'Economia e delle Finanze ed è stato istituito con la Legge 326/2003. La Fondazione ha l'obiettivo di promuovere l'eccellenza nella ricerca di base e in quella applicata e di favorire lo sviluppo del sistema economico nazionale. La costruzione dei laboratori iniziata nel 2006 si è conclusa nel 2009.

Lo staff complessivo di IIT conta circa 1440 persone. L’area scientifica è rappresentata da circa l’85% del personale. Il 45% dei ricercatori proviene dall’estero: di questi, il 29% è costituito da stranieri provenienti da oltre 50 Paesi e il 16% da italiani rientrati. Oggi il personale scientifico è composto da circa 60 principal investigators, circa 110 ricercatori e tecnologi di staff, circa 350 post doc, circa 500 studenti di dottorato e borsisti, circa 130 tecnici. Oltre 330 posti su 1400 creati su fondi esterni. Età media 34 anni. 41% donne / 59 % uomini.

Nel 2015 IIT ha ricevuto finanziamenti pubblici per circa 96 milioni di euro (80% del budget), conseguendo fondi esterni per 22 milioni di euro (20% budget) provenienti da 18 progetti europei17 finanziamenti da istituzioni nazionali e internazionali, circa 60 progetti industriali

La produzione di IIT ad oggi vanta circa 6990 pubblicazioni, oltre 130 finanziamenti Europei e 11 ERC, più di 350 domande di brevetto attive, oltre 12 start up costituite e altrettante in fase di lancio. Dal 2009 l’attività scientifica è stata ulteriormente rafforzata con la creazione di dieci centri di ricerca nel territorio nazionale (a Torino, Milano, Trento, Parma, Roma, Pisa, Napoli, Lecce, Ferrara) e internazionale (MIT ed Harvard negli USA) che, unitamente al Laboratorio Centrale di Genova, sviluppano i programmi di ricerca del piano scientifico 2015-2017.

IIT: the numbers

Istituto Italiano di Tecnologia (IIT) is a public research institute that adopts the organizational model of a private law foundation. IIT is overseen by Ministero dell'Istruzione, dell'Università e della Ricerca and Ministero dell'Economia e delle Finanze (the Italian Ministries of Education, Economy and Finance).  The Institute was set up according to Italian law 326/2003 with the objective of promoting excellence in basic and applied research andfostering Italy’s economic development. Construction of the Laboratories started in 2006 and finished in 2009.

IIT has an overall staff of about 1,440 people. The scientific staff covers about 85% of the total. Out of 45% of researchers coming from abroad 29% are foreigners coming from more than 50 countries and 16% are returned Italians. The scientific staff currently consists of approximately 60 Principal Investigators110 researchers and technologists350 post-docs and 500 PhD students and grant holders and 130 technicians. External funding has allowed the creation of more than 330 positions . The average age is 34 and the gender balance proportion  is 41% female against 59% male.

In 2015 IIT received 96 million euros in public funding (accounting for 80% of its budget) and obtained 22 million euros in external funding (accounting for 20% of its budget). External funding comes from 18 European Projects, other 17 national and international competitive projects and approximately 60 industrial projects.

So far IIT accounts for: about 6990 publications, more than 130 European grants and 11 ERC grants, more than 350 patents or patent applications12 up start-ups and as many  which are about to be launched. The Institute’s scientific activity has been further strengthened since 2009 with the establishment of 11 research nodes throughout Italy (Torino, Milano, Trento, Parma, Roma, Pisa, Napoli, Lecce, Ferrara) and abroad (MIT and Harvard University, USA), which, along with the Genoa-based Central Lab, implement the research programs included in the 2015-2017 Strategic Plan.