Direzione e uffici C.I.B.

Direzione CIB:
Prof. Claudio Schneider
Email: claudio.schneider@Lncib.it

Segreteria CIB:
Prof. Roberto Gambari
Email: roberto.gambari@unife.it

SEGRETERIA ORGANIZZATIVA:
Elisabetta Lambertini
Tel: 0532/974451
Fax: 0532/974484
E-mail: lmblbt@unife.it

AMMINISTRAZIONE:
Vanessa Florit
Area di Ricerca
Padriciano, 99 - 34012 Trieste
Tel: 040/398979
Fax: 040/398990
E-mail: cib@lncib.it

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Bossa Francesco Stampa
RESPONSABILE DELLA U. O.

Cognome e Nome Bossa Francesco
Qualifica PO
Facoltà Biotechnological Science
Dipartimento
Scienze Biochimiche
Settore Scientifico Disciplinare
BIO/10
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PERSONALE STRUTTURATO

Cognome e Nome Angelaccio Sebastiana
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Dipartimento
Scienze Biochimiche
Ente di appartenenza
Università La Sapienza
Cognome e Nome Barra Donatella
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PO
Dipartimento
Scienze Biochimiche
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Università La Sapienza
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Contestabile Roberto
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Scienze Biochimiche
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Università La Sapienza
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De Biase Daniela
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Scienze Biochimiche
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Università La Sapienza
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di Salvo Martino Luigi
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RU
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome
Franco Alessandra
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Tecnico
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome Giorgi Alessandra
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Tecnico Laureato
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Scienze Biochimiche
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Università La Sapienza
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Mangoni Maria Luisa
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RU
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Università La Sapienza
Cognome e Nome Maras Bruno
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Università La Sapienza
Cognome e Nome Miele Rossella
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Scienze Biochimiche
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Università La Sapienza
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Mignogna Giuseppina
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Scienze Biochimiche
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Università La Sapienza
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Paiardini Alessandro
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RU
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Università La Sapienza
Cognome e Nome Pascarella Stefano
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome
Schininà Maria Eugenia
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome
Tramonti Angela
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Ricercatore
Dipartimento
Istituto di Biologia e Patologia Molecolari
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CNR
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PERSONALE NON STRUTTURATO

Cognome e Nome
Bastianelli Daniela
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Dottorando
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome
Daidone Frederick
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Scienze Biochimiche
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Università La Sapienza
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Di Francesco Laura
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome Florio Rita
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Scienze Biochimiche
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Gentile Giovanna
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Marcellini Hercolani Gaddi Ludovica
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome Marsango Sara
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome
Pennacchietti Eugenia
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Scienze Biochimiche
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Università La Sapienza
Cognome e Nome Siglioccolo Alessandro
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Vivoli Mirella
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LINEE DI RICERCA

The activity of the group is focussed on diverse research lines whose common basis is the study of the structure-function relationship of proteins and bioactive peptides and the characterization of their properties and physiological role in particular systems of biotechnological and medical relevance.

The most traditional area of competence is the study and characterization of the pyridoxal-phosphate (PLP) dependent enzymes, particularly those of the fold type I, and the elucidation of their role in systems of potential biotechnological and biomedical impact. The dissection of the catalytic mechanism of several PLP enzymes and the analysis of their structure (e. g. serine hydroxymethyltransferase, GABA aminotransferase, glutamic decarboxylase, etc.) opens the possibility to engineer and modulate their activity and, therefore, to produce forms with novel functional and stability characteristics. Likewise, the knowledge of the detailed chemical properties can suggest how to design effective and specific inhibitors for specific PLP enzymes involved in metabolisms relevant for severe pathologies, like the serine hydroxymethyltrasferase for cancer and GABA aminotransferase for epilepsy. Expectedly, these inhibitors can reveal the way to the development of more effective drugs.

Fully integrated with the other research lines, is the in silico analysis of proteins to understand their chemical and conformational properties and their evolutionary and functional plasticity. Also to this respect, the PLP dependent enzymes form a very interesting family which is very ancient and, consequently, collects members which are very distantly related. We can therefore learn how the catalytic versatility of the PLP enzymes we know today could originate from an ancestral scaffold which underwent extensive remodelling during the divergent evolution without disruption of its basic architecture. The evolutionary story of the PLP enzymes can be archetypal of other protein families. Along the same lines, the wealth of structural information now available is exploited to understand the structural basis of the adaptation of several enzyme families (including the PLP enzymes) to extreme environmental conditions such as those experienced by the thermophilic or psychrophilic organisms. The group provides its expertise in bioinformatics also in the framework of collaborations with other groups of this and other universities.

Another research line involves the structural/functional characterization and mechanisms of action of antimicrobial peptides (AMPs) isolated from the skin of frogs as well as their role as effector molecules of innate immunity. AMPs are essential components of the innate immune system of all organisms and amphibian skin is one of the richest natural sources. The widespread and often empirical use of conventional antimicrobials has led to a drastic reduction in their therapeutic efficacy and to the emergence of resistance in a large number of microbes, which represent a serious life-threat. In addition, antibiotic therapy against Gram-negative bacteria is frequently associated with the release of their outer membrane components (endotoxin or lipopolysaccharide, LPS). LPS is a potent stimulator of immune cells and induces the secretion of several pro-inflammatory cytokines. Remarkably, when a prolonged activation of the immune system takes place, it leads to an unbalanced production of such cytokines, eventually resulting in the septic shock syndrome. Therefore, there is an urgent need to search for alternative anti-microbial agents to prevent resistance and with the potential to kill bacteria and to neutralize the toxic effects of LPS. Different from conventional antibiotics, which inhibit intracellular processes, cationic AMPs have the ability to select the target microorganism through electrostatic interactions with the anionic compounds of its cell surface (e.g. LPS) and to permeate the membrane, causing irreversible damage. Modes of action studies of AMPs in biological and artificial systems, such as those provided by model membranes, can open additional avenues for the discovery and development of new peptide-based anti-infective and anti-endotoxin drugs.

The research group spent during the past years many efforts to acquire expertise in the most recent and advanced techniques in the field of molecular biology, chemistry, analysis and purification of proteins. The availability of advanced equipment (protein sequencer, amino acid analyzers, mass spectrometers, etc.) supports the experimental research also in collaboration with many other research groups. Most recently, several research lines in the field of proteomics and genomics applied to biomedical research have been undertaken, such as the achievement of the inventory of the proteins expressed by Neisseria meningitidis, the structural characterization of peptides from Conus venom of potential pharmacological use, prion allotype profiling and set up of LC-MS methodologies for advanced clinical molecular diagnostics.

Substantial part of the research is represented by the attempt to engineer bacteria for the large-scale production of peptides or proteins of potential biotechnological use.

TECNOLOGIE IN POSSESSO DELL'U. O.

  • Enzyme kinetics analysis
  • Genetic engineering
  • Molecular graphics and in silico simulation of biological macromolecules
  • Mass spectrometry
  • Protein chemistry
  • Gene expression in heterologous systems
  • Regulation of gene expression
  • Liposome technology
  • In vitro antimicrobial assays

STRUMENTAZIONE

Denominazione
Struttura ove la strumentazione è allocata
Responsabile della strumentazione
ThermoElectron LCQ mass spectrometer equipped with an electrospray source and an ion trap analyser
Dipartimento di Scienze Biochimiche
M.E. Schininà
Applied Biosystems Voyager STR mass spectrometer equipped with a MALDI source and a ToF analyser
Dipartimento di Scienze Biochimiche
M.E. Schininà
Applied Biosystems Qtrap 2000 mass spectrometer interfaced with an Agilent HPLC
Dipartimento di Scienze Biochimiche, sede distaccata DiMA II Facoltà di Medicina, Ospedale S. Andrea
G. Gentile
Proteome station PF2D-HPLC
Dipartimento di Scienze Biochimiche, sede distaccata DiMA II Facoltà di Medicina, Ospedale S. Andrea
G. Gentile
Bio-Logic Chemical Quenched-flow
Dipartimento di Scienze Biochimiche Sede distaccata Via degli Apuli
R. Contestabile
Real-time PCR
Dipartimento di Scienze Biochimiche Sede distaccata di Latina Sede distaccata DiMA II Facoltà di Medicina, Ospedale S. Andrea
D. De Biase / G. Gentile
Absorbance and Fluorescence Microplate reader
Dipartimento di Scienze Biochimiche Sede distaccata Via degli Apuli
M.L. Mangoni
Fluorescence Microscope
Dipartimento di Scienze Biochimiche Sede distaccata Via degli Apuli
M.L. Mangoni
Modellizzazione molecolare e docking. Hardware -n°2 Mac Pro 8 Core 3.2 GHz -n°1 Server Dual Xeon 3.0 GHz -n°2 Dual Core Pentium 4 PC -n°1 Pentium 3 PC Software: -MOE 2008.10[CCG] -Molegro 2008.3.0.0 [Bioinformatics Solutions]
Dipartimento di Scienze Biochimiche Sede distaccata Via degli Apuli
S. Pascarella

PUBBLICAZIONI

Pennacchietti E, Lammens TM, Capitani G, Franssen MC, John RA, Bossa F, De Biase D. Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH. J Biol Chem. 2009 Nov 13;284(46):31587-96. Epub 2009 Sep 21.

Musayev FN, Di Salvo ML, Saavedra MA, Contestabile R, Ghatge MS, Haynes A, Schirch V, Safo MK. Molecular basis of reduced pyridoxine 5'-phosphate oxidase catalytic activity in neonatal epileptic encephalopathy disorder. J Biol Chem. 2009 Nov 6;284(45):30949-56. Epub 2009 Sep 15.

Siglioccolo A, Bossa F, Pascarella S. Structural adaptation of serine hydroxymethyltransferase to low temperatures. Int J Biol Macromol. 2009 Oct 6. [Epub ahead of print]

Giorgi A, Di Francesco L, Principe S, Mignogna G, Sennels L, Mancone C, Alonzi T, Sbriccoli M, De Pascalis A, Rappsilber J, Cardone F, Pocchiari M, Maras B, Schininà ME. Proteomic profiling of PrP27-30-enriched preparations extracted from the brain of hamsters with experimental scrapie. Proteomics. 2009 Aug;9(15):3802-14.

Severino V, Paiardini A, Pascarella S, Parente A, Chambery A. Structural analysis of toxic volkensin, a type 2 ribosome inactivating protein from Adenia volkensii Harm (kilyambiti plant): molecular modeling and surface analysis by computational methods and limited proteolysis. Int J Biol Macromol. 2009 Nov 1;45(4):407-13. Epub 2009 Jul 8.

Marcellini L, Borro M, Gentile G, Rinaldi AC, Stella L, Aimola P, Barra D, Mangoni ML. Esculentin-1b(1-18)--a membrane-active antimicrobial peptide that synergizes with antibiotics and modifies the expression level of a limited number of proteins in Escherichia coli. FEBS J. 2009 Oct;276(19):5647-64. Epub 2009 Sep 2.

Misiti S, Stigliano A, Borro M, Gentile G, Michienzi S, Cerquetti L, Bucci B, Argese N, Brunetti E, Simmaco M, Toscano V. Proteomic profiles in hyperandrogenic syndromes. J Endocrinol Invest. 2009 Oct 9. [Epub ahead of print]

Marsango S, di Patti MC, Barra D, Miele R. The Bv8 gene from Bombina orientalis: molecular cloning, genomic organization and functional characterization of the promoter. Peptides. 2009 Dec;30(12):2182-90. Epub 2009 Sep 10.

Tramonti A, De Canio M, De Biase D. GadX/GadW-dependent regulation of the Escherichia coli acid fitness island: transcriptional control at the gadY-gadW divergent promoters and identification of four novel 42 bp GadX/GadW-specific binding sites. Mol Microbiol. 2008 Nov;70(4):965-82. Epub 2008 Sep 18.

Vivoli M, Angelucci F, Ilari A, Morea V, Angelaccio S, di Salvo ML, Contestabile R. Role of a conserved active site cation-pi interaction in Escherichia coli serine hydroxymethyltransferase. Biochemistry. 2009 Dec 22;48(50):12034-46.

DOTTORATI DI RICERCA

Componente U.O. Dottorato di Ricerca Coordinatore Sede
Bossa Francesco
Biochimica
Paolo Sarti
Dip. Scienze Biochimiche
Donatella Barra
Biochimica
Paolo Sarti
Dip. Scienze Biochimiche
Pascarella Stefano
Biofisica
Alfredo Colosimo
CISB

CONGRESSI C.I.B.

Congressi Partecipazione
CNB4

CNB5

CNB6

CNB7

CNB8

CNB9
CNB10