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Gianpiero Garau

Researcher
Group Leader - BIOSTRUCTUREs Lab

Research Line

Electron Crystallography

Center

CNI@NEST Pisa

Contacts

ISTITUTO ITALIANO DI TECNOLOGIA (IIT CNI@NEST) Piazza S.Silvestro 12 - Pisa (Italy).
+39 050 509379
Contact Me

About

 

 

BIOSTRUCTUREs Lab

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

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

Email:
gianpiero.garau@iit.it

 

The research in my lab aims to generate by protein engineering novel bioinspired 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. Applications can range from design of bioactive 3D nano-biomaterials to cascade biocatalysis in sustainable technology, from bioelectronics to biomolecular medicine. 

Our research interests also focus on structure-function relationships and interactions of innovative membrane protein targets, relevant for metabolic and eating disorders, 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)

 

POST DOC POSITION NOW AVAILABLE  (Posted: Oct 2019)

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

 

GARAU_Foto_Gruppo_Biostructures_small.jpg


Interests

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

Projects

 

 

> 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

 

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> 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) [ http://www.esteri.it/mae/en ] ( 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) [ http://cordis.europa.eu/result/rcn/141649_en.html ].

 

 Cover_ACS CHEM Biol_2016.jpg
 
 

JOURNAL COVER

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

http://pubs.acs.org/toc/acbcct/11/10

FEATURED ARTICLES

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

http://www.cell.com/structure/abstract/S0969-2126%2815%2900005-2 

HIGHLIGHTS

  • CELL CHEMICAL BIOLOGY (Cell Press): Bile Acids as Enzyme Regulators

http://www.cell.com/chemistry-biology/fulltext/S1074-5521(15)00120-9

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

https://www.elettra.trieste.it/it/lightsources/elettra/elettra-beamlines/xrd1/xrdhighlights/page-9.html?showall=

  • 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

http://cordis.europa.eu/result/rcn/148980_en.html

 
 
 
 
 

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: 

https://scholar.google.it/citations?user=oss1OmMAAAAJ&hl=en&cstart=0&pagesize=20

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