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Gianpiero Garau Write a Message

Researcher
Group Leader

Center

CNI@NEST Pisa

Contacts

Center for NanoTechnology Innovation@NEST, Piazza S.Silvestro - PISA

https://www.iit.it/people/gianpiero-garau

+39 010 71781 574

+39 050 509379

About

NanoBioStructures Lab - Email: gianpiero.garau@iit.it

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

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

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NanoBioStructures

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.

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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.

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

DOTTORATO DI RICERCA in NANOSCIENZE @ SCUOLA NORMALE SUPERIORE, Pisa (Italia) 2017

http://phd.sns.it/it/nanosciences/

NanoBioSTRUCTURES

Informal enquires may be made to Gianpiero Garau (gianpiero.garau@iit.it)

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

Projects

> 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

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> NAPE-PLD

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).

http://cordis.europa.eu/result/rcn/141649_en.html

JOURNAL COVER

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

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

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:

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

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