• Istituto di Biologia e Patologia Molecolari


Tel :+393490739979
Fax :+39064440062
alberto.boffi@uniroma1.it
ALBERTO BOFFI
Full Professor

Department of Biochemical Sciences -A. Rossi Fanelli.
Sapienza University of Rome
Edificio di Chimica Biologica Piano terra, stanza T16 P.le A. Moro 5 - 00185 Roma

The research activity within IBPM has been focussed on structural biology of redox proteins and enzymes with applications in synthetic biology and green chemistry. In particular, modern protein engineering methods have been applied to selected enzymes in order to obtained improved catalytic activities or enhanced solubilities thus providing a platform for the development of novel tools in complex organic synthesis. In very recent years, the same strategy has been applied to human proteins (ferritins and globins) in order to obtain efficient and versatile carriers for targeted drug delivery in diagnostic and therapeutic applications.

1. Ilari A, Baiocco P, Messori L, Fiorillo A, Boffi A, Gramiccia M, Di Muccio T, 

Colotti G. A gold-containing drug against parasitic polyamine metabolism: the

X-ray structure of trypanothione reductase from Leishmania infantum in complex

with auranofin reveals a dual mechanism of enzyme inhibition. Amino Acids. 2012

Feb;42(2-3):803-11. 

 

2. Fiorillo A, Federico R, Polticelli F, Boffi A, Mazzei F, Di Fusco M, Ilari A, 

Tavladoraki P. The structure of maize polyamine oxidase K300M mutant in complex

with the natural substrates provides a snapshot of the catalytic mechanism of

polyamine oxidation. FEBS J. 2011 Mar;278(5):809-21. 

 

3. Ilari A, Franceschini S, Bonamore A, Arenghi F, Botta B, Macone A, Pasquo A,

Bellucci L, Boffi A. Structural basis of enzymatic (S)-norcoclaurine

biosynthesis. J Biol Chem. 2009 Jan 9;284(2):897-904. 

 

4. Ilari A, Boffi A. Structural studies on flavohemoglobins. Methods Enzymol.

2008;436:187-202. 

 

5. Ilari A, Bonamore A, Franceschini S, Fiorillo A, Boffi A, Colotti G. The X-ray

structure of N-methyltryptophan oxidase reveals the structural determinants of

substrate specificity. Proteins. 2008 Jun;71(4):2065-75. 

 

6. Bonamore A, Attili A, Arenghi F, Catacchio B, Chiancone E, Morea V, Boffi A. A

novel chimera: the "truncated hemoglobin-antibiotic monooxygenase" from

Streptomyces avermitilis. Gene. 2007 Aug 15;398(1-2):52-61. Epub 2007 May 3.

 

7. Ilari A, Kjelgaard P, von Wachenfeldt C, Catacchio B, Chiancone E, Boffi A.

Crystal structure and ligand binding properties of the truncated hemoglobin from 

Geobacillus stearothermophilus. Arch Biochem Biophys. 2007 Jan 1;457(1):85-94.

 

8. Boffi A, Cacchi S, Ceci P, Cirilli R,  Fabrizi  G Prastaro A, Niembro S, Shafir A, Vallribera A The Heck Reaction of Allylic Alcohols Catalyzed by Palladium Nanoparticles in Water: Chemoenzymatic Synthesis of (R)-(−)-Rhododendrol. ChemCatChem 2010 63 1224-29.

 

9. Prastaro A, Ceci P, Chiancone E, Boffi A, Fabrizi G, Cacchi S. Homocoupling of arylboronic acids and potassium aryltrifluoroborates catalyzed by protein-stabilized palladium nanoparticles under air in water. Tetrahedron Lett. 2010 51 2550–2552.

 

10. Prastaro A, Ceci P, Chiancone E, Boffi A, Cirilli R, Colone M, Fabrizi G, Stringaro A, Cacchi S. Suzuki-Miyaura cross-coupling catalyzed by protein-stabilized palladium nanoparticles under aerobic conditions in water: application to a one-pot chemoenzymatic enantioselective synthesis of chiral biaryl alcohols. Green Chem. 2009 11 1929-1931.

 

Alberto Boffi started his career at the Department of Biochemical Sciences of the University "La Sapienza" in Rome, where he was involved in the study of structure function relationships in heme proteins by physico-chemical methods. The research activity led to the publication of 107 scientific papers on international peer reviewed journals (IF > 420, HI = 22) and to establish close collaborations and period of research activity in the following laboratories:

- Laboratoire de Oceanologie, Université de Luminy II, Marseille, France (1986-1988).

- Duke University Marine Laboratory, Beaufort (NC), USA (1988).

- AT&T Bell Laboratories, Murray Hill (NJ), USA (1991-1996).

- Albert Einstein College of Medicine (NY), USA (1991-).

- INFM ed Istituto di Fisica dell’Università di Palermo (1993-).

The present research activities are focussed on:

- Structure and function of novel hemeproteins.  Novel hemeproteins from procariots have been identified cloned and expressed, their structure and catalytic activities have been determined. 

- Protein engineering for drug delivery. This line of research involves the application of protein engineering methods for the development of protein based drug delivery systems.

- Biocatalysis. The application of heme and flavin enzymes to biotransformations has recently been focussed on oxidation processes of industrial relevance.

 

Selected Publications (10 max, in collaboration with IBPM researchers)