Barbara Spolaore

Department of Pharmaceutical and Pharmacological Sciences, University of Padova
via F. Marzolo 5, 35131 Padova - Italy
Current Position:
Assistant Professor of Biochemistry (SSD BIO/10)

Phone: +39-049-827-5702

  Short CV

Born in Mirano (VE), Italy on the 7th May 1974

1999: Degree summa cum laude in Chemistry and Pharmaceutical Technology, University of Padua

1999-2002: PhD in Pharmaceutical Sciences, Dept. of Pharmaceutical and Pharmacological Sciences, University of Padua (Supervisor: Prof. A. Fontana).

2003-2008: Post-doctoral Fellow at the “Centro di Ricerca Interdipartimentale per le Biotecnologie Innovative” (CRIBI), University of Padua (Supervisor: Prof. A. Fontana).

2005: European doctorate in biotechnology (EDBT) awarded by the European Association for Higher Education in Biotechnology (HEduBT).

2008- : Assistant Professor of Biochemistry (SSD BIO/10)

2014: Italian National Academic Qualification as Associate Professor of Biochemistry (SSD BIO/10)- call 2012.


  Office hours

Upon appointment

  Availability for Thesis Projects

Disponibili due posti di internato di Tesi di Laurea Magistrale per studenti di CTF, Farmacia e Pharmaceutical Biotechnologies da MARZO 2023. Il progetto di Tesi verterà sullo studio della conformazione e dinamica di proteine allo scopo di chiarire variazioni conformazionali che causano determinati stati patologici. Le tecniche utilizzate nel progetto riguarderanno la caratterizzazione chimica delle proteine mediante RP-HPLC e spettrometria di massa e la caratterizzazione conformazionale di proteine mediante tecnica di scambio idrogeno-deuterio e spettrometria di massa e mediante tecniche spettroscopiche (dicroismo circolare e fluorescenza).


  Scientific Activities

During the PhD and the post-doctoral period, I worked on the conformational characterization of proteins by means of spectroscopic techniques and by combining limited proteolysis and mass spectrometry. Our group studied the conformational changes determined on model proteins and on proteins of pharmaceutical interest by particular solvent conditions and by the interaction with ligands or fatty acids.

My scientific interests are still in the field of the chemical and conformational characterization of proteins, mainly by exploiting mass spectrometry techniques. Recently,  I focused on microbial transglutaminase (TGase), an enzyme that allows the site-specific derivatization of proteins at the level of Lys or Gln residues often without affecting protein structure and function. We investigated if the conformational features of the protein substrate determine the sites of TGase derivatization and we used this enzyme to modify proteins with fluorophores, chelating agents or other compounds to enable a range of biotechnological applications.

Currently, we are implenting the hydrogen-deuterium eschange mass spectrometry technique (HDX-MS)  that allows mapping of protein conformation in solution under physiological conditions using small amounts of material. We apply this methodology on different protein systems of physio-pathological relevance, that are under study in our laboratory or in on-going collaborations.

  Technical expertise

Electrospray mass spectrometry (MS) and LC-MS/MS applied to the analysis of proteins. Analysis of protein structure and dynamics by hydrogen-deuterium exchange mass spectrometry. Spectroscopic techniques: UV-visible spectroscopy, circular dichroism, fluorescence.Chromatographic techniques useful for protein purification and characterization. Gel electrophoresis. Chemical and enzymatic hydrolysis of proteins in solution or in gel.


  1. Montalbán-López, M., Spolaore, B., Pinato, O., Martínez-Bueno, M., Valdivia, E., Maqueda, M., and Fontana, A. (2008) Characterization of linear forms of the circular enterocin AS-48 obtained by limited proteolysis. FEBS Lett. 582, 3237–3242.
  2. Mero, A., Spolaore, B., Veronese, F. M. and Fontana, A. (2009). Transglutaminase-mediated PEGylation of proteins: direct identification of the sites of protein modification by mass spectrometry using a novel monodisperse PEG. BIOCONJUG. CHEM. 20, 384–389.
  3. Spolaore, B., Raboni, S., Ramos Molina, A., Satwekar, A., Damiano, N., and Fontana, A. (2012) Local Unfolding Is Required for the Site-Specific Protein Modification by Transglutaminase. BIOCHEMISTRY 51, 8679-8689.
  4. Spolaore, B., Damiano, N., Raboni, S., and Fontana, A. Site-specific derivatization of avidin using microbial transglutaminase. (2014) BIOCONJUG. CHEM. 25(3): 470-480.
  5. Antoniel, M., Jones, K., Antonucci, S., Spolaore, B.,Fogolari, F., Petronilli, V., Giorgio, V., Carraro, M., Di Lisa, F., Forte, M., Szabó, I., Lippe, G., and Bernardi, P. (2018) The unique histidine in OSCP subunit of F-ATP synthase mediates inhibition of the permeability transition pore by acidic pH. EMBO REP. 19(2): 257-268.
  6. Spolaore, B., Forzato, G., and Fontana, A. (2018) Site-specific derivatization of human interferon β-1a at lysine residues using microbial transglutaminase. AMINO ACIDS 50(7): 923-932.
  7. Massimino, M.L., Simonato, M., Spolaore, B., Franchin, C., Arrigoni, G., Marin, O., Monturiol-Gross, L., Fernández, J., Lomonte, B., and Tonello, F. (2018) Cell surface nucleolin interacts with and internalizes Bothrops asper Lys49 phospholipase A2 and mediates its toxic activity. SCI REP. 8(1): 10619.


Title: "Method for Labeling of Sensitive and Thermosensitive Targeting Biomolecules with Technetium based Compounds"

Inventor(s): Bolzati Cristina; Salvarese Nicola; Refosco Fiorenzo; Ghiani Simona; Maiocchi Alessandro; Spolaore Barbara


International Publication Number: WO/2018/109164

  Research projects and Funds

2018-2020: PRID-2018, DSF-Principal investigator

Application of Hydrogen Exchange Mass Spectrometry in Molecular Medicine

Probing Protein Structure and Dynamics in Protein Systems of Biopharmaceutical Interest