POLLEGIONI LOREDANO


Responsabile dell'U.O.

Cognome e Nome

POLLEGIONI LOREDANO

Qualifica

PO

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Settore scientifico disciplinare

BIO/10

E-mail

loredano.pollegioni@uninsubria.it

Telefono

Personale strutturato

Cognome e Nome

GIANLUCA MOLLA

Qualifica

PA

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Cognome e Nome

LUCIANO PIUBELLI

Qualifica

Ricercatore

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Cognome e Nome

SACCHI SILVIA

Qualifica

PA

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Cognome e Nome

CALDINELLI LAURA

Qualifica

Technician

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Cognome e Nome

ELENA ROSINI

Qualifica

Ricercatore

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Personale non strutturato

Cognome e Nome

CAPPELLETTI PAMELA

Qualifica

Post-doc

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Cognome e Nome

TONIN FABIO

Qualifica

Ph.D student

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Cognome e Nome

MELIS ROBERTA

Qualifica

Ph.D student

Dipartimento

DEPARTMENT OF BIOTECHNOLOGY AND LIFE SCIENCES

Ente di appartenenza

UNIVERSITY OF INSUBRIA

Linee di ricerca

The research activity of this U.O. is mainly focused on: 1) protein engineering applied to industrial enzymology and to medical biotechnology, 2) the investigation of the life basis of the human pathologies, 3) elucidation of the role of D-amino acids on neurotransmission. The wide experience acquired in the past years in resolving, identifying, and characterising proteins, introduced our research group in the functional post-genomics and protein engineering fields. At present the laboratory is engaged in the cloning and characterisation of proteins involved in human pathologies and production of enzymes relevant for biotechnological applications with novel functional properties. The main goals of our biotechnological projects are: - Cloning and overexpression in microorganisms of genes encoding for enzymes used in industrial applications. - Protein engineering of flavoenzymes to produce mutants for specific biotechnological applications using two different approaches: rational design (by site directed mutagenesis) and directed evolution (by random mutagenesis, screening and mutants selection). - Production and purification of recombinant proteins or native proteins, downstream processing and scaling-up studies. - Covalent immobilization of enzymes on different matrixes to be employed in bioreactors. - Set-up of bioconversion processes to produce fine chemicals. - Development of biosensors to detect and quantify D-amino acids in food and biological samples. - Gene therapy of solid tumors using D-amino acid oxidase from R. gracilis as prodrug converter (oxidative stress therapy mediated by hydrogen peroxide). – Investigation of the life basis of schizophrenia (modulation of D-serine concentration in human brain). - Investigation of the role of D-serine and D-aspartate on brain functions (and pathologies).

Tecnologie in uso dall'UO

  1. 1.
    Industrial enzymology
  2. 2.
    Protein engineering (SDM and directed evolution)
  3. 3.
    Protein expression, purification and downstream processing
  4. 4.
    Enzyme immobilization techniques
  5. 5.
    Immunolocalization
  6. 6.
    Transient kinetics techniques, protein-protein interactions
  7. 7.
    Neurotransmission
  8. 8.
    Fermentation technologies, cell cultures
  9. 9.
    Bioreactors and bioconversions optimisation
  10. 10.
    Bioinformatics and molecular modelling

Strumentazione

Denominazione

Stopped-flow spectrofluorimeter
Modulable fermentor (2 & 10 l)
Äkta chromatography systems
epMotion 5075 liquid handler
HPLC Jasco
Sorvall Centrifuge
Beckman Centrifuge
UV-Vis Jasco Spectrophotometers
CD Spectrophotometers Jasco J-815

Struttura ove la strumentazione è allocata

DBSV
DBSV
DBSV
DBSV
DBSV
DBSV
DBSV
DBSV
DBSV

Responsabile

G. Molla
G. Molla
L. Piubelli
E. Rosini
L. Caldinelli
L. Caldinelli
L. Caldinelli
L. Piubelli
L. Piubelli

Pubblicazioni

  1. 1.
    Pollegioni L, Molla G.2011 New biotech applications from evolved D-amino acid oxidases. Trends Biotechnol. 29(6):276-283.
  2. 2.
    Papouin T, Ladépêche L, Ruel J, Sacchi S, Labasque M, Hanini M, Groc L, Pollegioni L, Mothet JP, Oliet SH. Synaptic and Extrasynaptic NMDA Receptors Are Gated by Different Endogenous Coagonists. Cell. 2012 150(3):633-46.
  3. 3.
    Caldinelli L, Sacchi S, Molla G, Nardini M, Pollegioni L.Characterization of human DAAO variants potentially related to an increased risk of schizophrenia. Biochim Biophys Acta Mol. Basis Diseases. 2013;1832(3):400-10.
  4. 4.
    Golden E, Paterson R, Tie WJ, Anandan A, Flematti G, Molla G, Rosini E, Pollegioni L, Vrielink A. Structure of a class III engineered cephalosporin acylase: comparisons with class I acylase and implications for differences in substrate specificity and catalytic activity. Biochem J. 2013 451(2):217-26.
  5. 5.
    Li Y, Sacchi S, Pollegioni L, Basu AC, Coyle JT, Bolshakov VY. Identity of endogenous NMDAR glycine site agonist in amygdala is determined by synaptic activity level. Nat Commun. 2013 4:1760
  6. 6.
    Hopkins SC, Heffernan ML, Saraswat LD, Bowen CA, Melnick L, Hardy LW, Orsini MA, Allen MS, Koch P, Spear KL, Foglesong RJ, Soukri M, Chytil M, Fang QK, Jones SW, Varney MA, Panatier A, Oliet SH, Pollegioni L, Piubelli L, Molla G, Nardini M, Large TH. Structural, Kinetic, and Pharmacodynamic Mechanisms of D-Amino Acid Oxidase Inhibition by Small Molecules. J Med Chem. 2013 56(9):3710-24.
  7. 7.
    Rosini E, Piubelli L, Molla G, Frattini L, Valentino M, Varriale A, D'Auria S, Pollegioni L. Novel biosensors based on optimized glycine oxidase. 2014 FEBS J. 281(15):3460-
  8. 8.
    Le Bail M, Martineau M, Sacchi S, Yatsenko N, Radzishevsky I, Conrod S, Ait Ouares K, Wolosker H,Pollegioni L, Billard JM, Mothet JP.Identity of the NMDA receptor coagonist is synapse specific and developmentally regulated in the hippocampus. Proc Natl Acad Sci U S A. 2015 Jan 13;112(2):E204-13.
  9. 9.
    Molla G, Nardini M, Motta P, D'Arrigo P, Panzeri W, Pollegioni L. Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins. Biochem J. 2014, 464(3):387-99.
  10. 10.
    Pollegioni L, Tonin F, Rosini E. Lignin-degrading enzymes. FEBS J. 2015 282(7):1190-213.

Dottorandi di ricerca

Componente UO

Loredano Pollegioni
Luciano Piubelli
Gianluca Molla
Silvia Sacchi

Dottorato di ricerca

Biotecnologie, Bioscienze e Tecnologie Chirurgiche
Biotecnologie, Bioscienze e Tecnologie Chirurgiche
Biotecnologie, Bioscienze e Tecnologie Chirurgiche
Biotecnologie, Bioscienze e Tecnologie Chirurgiche

Coordinatore

Loredano Pollegioni
Loredano Pollegioni
Loredano Pollegioni
Loredano Pollegioni

Sede

Varese - DBSV
Varese - DBSV
Varese - DBSV
Varese - DBSV