Group Leader - BIOSTRUCTUREs Lab
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, x-ray diffraction & electron crystallography, single particle cryo-electron microscopy, mass spectrometry, surface plasmon resonance, microcalorimetry, supported by computational methods. These methods allow us to describe the details of biomolecular structures, and the thermodynamics and kinetics of protein interactions.
Gianpiero Garau (P.I.)
Eleonora Margheritis (postdoc)
Valentina De Lorenzi (postdoc),
Sara Chiarugi (PhD fellow)
Elisa Martino (PhD fellow)
Aurora Russo (student).
> 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 FOUNDATION IN EUROPE.
> 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 ].
- 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
- Nanobeam precession-assisted 3D electron diffraction reveals a new HEWL polymorph
Lanza A, Margheritis E, Mugnaioli E, Valentina C, Garau G, Gemmi M
2018 IUCrJ DOI:https://doi.org/10.1107/S2052252518017657.
- 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.
- 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.
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