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Gianpiero Garau Write a Message

Group Leader




Center for NanoTechnology Innovation@NEST, Piazza S.Silvestro - PISA
+39 010 71781 574
+39 050 509379


NanoBioStructures Lab  - Email:

Center for Nanotechnology Innovation@NEST - Scuola Normale Superiore, Pisa

Department of Drug Discovery - Italian Institute of Technology (IIT)




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 nanobiostructures, such as biomolecular cages and crystals. This process is strongly driven by specific technological needs. Engineering protein molecules that self-assemble into complex bioarchitectures is an innovative goal of nanobiotechnology. Applications can range from design of bioactive 3D nanobiomaterials to nanobiosensors, from bioelectronics to biomedicine.
My research interests also focus on the relationships 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 Biology, Biochemistry, and Molecular Biophysics. These methods provide insights into protein structure/dynamics and thermodynamics/kinetics of protein interactions (mainly, X-ray crystallography, SAXS, CryoEM/TM, Neutron Scattering, SPR, ITC and DSC, supported by protein engineering and computational approaches). We have contributed to the discovery of inhibitors/agonists for relevant metallo protein targets, and the development of GFP-based nano-biosensors, binding peptides, and low immunogenic cytokines for therapy.
Dr Garau is author and co-author of more than 40 publications (12 as first-author) in high quality journals (including JACS, Structure, PNAS, Nature Neuroscience), and a book chapter (X-ray Structures and Mechanisms of Metallo-Beta-Lactamases). His work has been presented in several international congresses as oral communications and abstracts. Main bragging rights include 2 Marie Curie fellow grants and 1 Marie Curie as project supervisor. He is depositor of dozens of structures in Protein Data Bank (PDB) and Cambridge Structural Database (CSD). He has access to major EU research platforms of synchrotron light source (ESRF, ELETTRA, DIAMOND) and Neutron Scattering (ILL) for Structural Biology.
Dr Garau is member of the European Crystallography Association, Italian Crystallography Association, and Italian Soc. of Biophysics SIBPA. Dr Garau is also reviewer for several scientific journals including PLoS ONE and Bioorg Med Chem, and Expert Evaluator of Marie Skłodowska-Curie Actions [call H2020].

BIO: After fellow studies in Protein Chemistry at the Science Park of Århus (Denmark), Dr Garau obtained his PhD in Chemistry from the University of Trieste (Italy). He worked as Postdoc at the Jean-Pierre Ebel Structural Biology Institute of Grenoble (France), at the European Synchrotron Radiation Facility (ESRF), and at the San Raffaele Biomedical Science Park, Milan (Italy). Before joining the Italian Institute of Technology (IIT), he was Assistant Specialist at the University of California, Irvine (USA), Dept of Pharmacology.




PhD Opportunities in NANOSCIENCES @ Scuola Normale Superiore, Pisa (ITALY)   2017




  • NanoBioSTRUCTURES       

             Informal enquires may be made to Gianpiero Garau (

             DEADLINE June 19 2017. Please, find the attached document below. 



> NanoBioStructures

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.


crystal cage small



The membrane-associated enzyme NAPE-PLD generates bioactive lipid amides that play important roles in stress and pain response, appetite and lifespan. Our structural and biophysical studies have shown the molecular process involved and have unveiled that the natural bile acids drive it. This discovery brings together bile acid physiology and lipid amide signaling, thus 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.


foglia e mano


This project is carried out with financial support from the EU (FP7 N. 268385).



  • CHEMICAL BIOLOGY (ACS): Bile Acids 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


  • 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
    ACS Chem Biol. 2016, 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
    J Mater Chem B 2016,
  • 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
    Exp Neurol. 2015, 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
    Structure 2015, 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
    J Am Chem Soc. 2013, 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
    Nature Neurosci. 2011, 15:64-69.
  • Energy Landscapes Associated with Macromolecular Conformational Changes from Endpoint Structures.
    Fornili A, Giabbai B, Garau G, Degano M
    J Am Chem Soc. 2010, 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
    Biophys J. 2007, 93:232-244.
  • Structural basis for mammalian vitamin B12 transport by transcobalamin.
    Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L
    Proc Natl Acad Sci U S A. 2006, 103:4386-4391.
  • 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
    J Biol Chem. 2005, 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
    J Mol Biol. 2005, 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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Accetta e chiudi

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.