NATALELLO ANTONINO

Ruolo:
Professore associato
Settore scientifico disciplinare:
Fisica per le scienze della vita, l'ambiente e i beni culturali (PHYS-06/A)
Gruppo scientifico disciplinare:
FISICA PER LE SCIENZE DELLA VITA, L'AMBIENTE E I BENI CULTURALI, DIDATTICA E STORIA DELLA FISICA (02/PHYS-06)
Stanza:
  • U03, Piano: 4, Stanza: 4050
  • U03, Piano: 4, Stanza: 4051

Biografia

PRESENT POSITION

Since September 2018: Associate professor of APPLIED PHYSICS at the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy. A. Natalello obtained the National Scientific Qualification (Abilitazione Scientifica Nazionale) for Full Professor of Applied Physics on December 2017.

 

EDUCATION

  • 2002: Laurea (Master Degree) in Industrial Biotechnology (110/110 cum laude), University of Milano-Bicocca, Milan, Italy.
  • 2006: PhD in Industrial Biotechnology, University of Milano-Bicocca, Italy. Title of the Thesis “Protein stability and aggregation studied by biophysical methods” (Supervisor: Prof. S. M. Doglia).
  • February 2005-Jun 2005: visiting scientist/PhD student at the Institute of Organic Chemistry of the Johannes Kepler University (Linz, Austria) performing research activities on mass spectrometry for protein studies.

 

PREVIOUS POSITIONS

  • Since September 2018: Associate Professor of APPLIED PHYSICS at the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy.
  • 2015-2018: Temporary Assistant Professor (RTD b - art. 24, comma 3, lettera b, legge 240/2010) of APPLIED PHYSICS at the Biophysics laboratory of the Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy
  • 2013-2015: postdoctoral fellow, Department of Physics, University of Milano-Bicocca, Milan, Italy.
  • 2008-2012: postdoctoral fellow, Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy.
  • 2007: research fellow from “Regione Lombardia”, Department of Biotechnology and Biosciences, University of Milano-Bicocca.

 

TEACHING ACTIVITIES

• 2002-2014 Tutor in teaching laboratories for general and organic chemistry (First level degrees in Biotechnology and Biology).

• Since 2015, Biophysics /Spectroscopy for biotechnology (First level degree in Biotechnology)

• Since 2019, General Physics (First level degree in Biotechnology)

 

MEMBERSHIP OF SCIENTIFIC SOCIETIES        

• SIF - Società Italiana di Fisica

• SIBPA - Società Italiana di Biofisica Pura e Applicata

 

PUBLICATIONS

• >108 publications on peer-reviewed, international journals;

• total citations (March 2023): >4000 in Google Scholar; >3200 in Scopus;

• h-index (March 2023): h=39 (Google Scholar); h=33 (Scopus).

• 9 chapters on international books;

• > 60 participations to national and international congresses.

Google Scholar: https://scholar.google.com/citations?hl=it&user=CQkk38UAAAAJ

ORCID: https://orcid.org/0000-0002-1489-272X

 

Ricerca

Scientific interests

-Protein stability, aggregation, interactions. Major research topics: protein stability; amyloid aggregation; structure-function relation; aggregation of recombinant proteins; protein-protein and protein-ligand interactions; nano- and bio-materials.

-Bioanalytical applications of spectroscopic methods. Major research topics: FTIR (micro)spectroscopy of complex biological systems; in situ studies of biological processes; spectroscopic markers.

These topics are investigated by several biophysical approaches, among them: infrared spectroscopy and microspectroscopy (FTIR and microFTIR), fluorescence and circular dichroism (CD) spectroscopies, “Native” mass spectrometry, Isothermal Titration Calorimetry (ITC), and Surface Plasmon Resonance (SPR) spectroscopy. In particular, we have investigated several aspects of protein aggregation processes also considering their biomedical and biotechnological implications, as the in vivo formation of inclusion bodies in bacterial cells and the investigation of amyloid formation in vitro and in situ. Great experience has been acquired in this field thanks to the analysis of several proteins and peptides in vitro and in complex biological systems (such as intact cells and human tissues). In the framework of the Cariplo Foundation granted project “Structure-function relation of amyloid”, we developed an isotope edited FTIR approach to investigate the role of mutations and of a molecular chaperone on the misfolding and co-aggregation of human β-2 microglobulin variants. This approach allowed studying simultaneously the conformational properties of the isotopically labelled (13C) and unlabelled protein (12C) variants (at the same time) when co-present in the same sample. In particular, the sequence of events occurring during the co-polymerization of the D76N variant and wild type β-2 microglobulin and the effect of the chaperon crystallin in the aggregation process were characterized (Natalello et al. 2016 J. Biol. Chem. 291, 9678-9689, in collaboration with Prof. V. Bellotti, University of Pavia).The role of glutamine (Q) side chains in the two aggregation stages of the poly-Q protein Ataxin-3 was also studied by biophysical approaches. In particular, by H/D exchange experiments we showed for the first time that an IR marker band can be ascribed to glutamine side-chain hydrogen bonding (Natalello et al. 2011, PLoS One. 6:e18789). This IR marker band was employed in several subsequent publications to monitor the formation of mature poly-Q aggregates in vitro and in ex vivo protein samples (in collaboration with Prof. M.E. Regonesi, UniMiB).

 

In situ studies of amyloid deposits and the comparison of ex vivo and in vitro fibrils have been also performed in different systems, including pathogenic immunoglobulin light chains derived from patients (see “Ami et al. 2016 Sci Rep. 6:29096” and “Ami et al. 2019 Anal. Chem. 91, 2894–2900”). In particular, FTIR spectroscopy is a label-free and non-invasive approach that we apply not only to isolated biomolecules but also to intact cells and tissues. In our studies, we combine IR spectroscopy with multivariate analysis to obtain a “spectroscopic fingerprinting” of the sample under investigation, which represents a snapshot of the composition and structure of its main biomolecules. For instance, we applied this approach to fat aspirates from patients affected by systemic amyloidosis (Ami et al. 2019 Anal. Chem. 91, 2894–2900) and to tears from patients affected by amyotrophic lateral sclerosis (Ami et al. 2021 Anal. Chem. 93, 51, 16995–17002). In both systems, we found that our approach differentiates the samples from the diseased individuals from control specimens with high sensitivity and specificity. It is worth noting that the wavenumbers most important for discrimination allowed us to disclose spectroscopic markers related to the pathological molecular mechanisms.

 

 

Team

Ami Diletta – PostDoc Fellow
room 4051/4050, IV floor , building U3
tel: +39 02 6448 3461/3459
[email protected]
 

 

Pubblicazioni

  • Natalello, A., Mangione, P., Giorgetti, S., Porcari, R., Marchese, L., Zorzoli, I., et al. (2016). Co-fibrillogenesis of wild-type and D76N β2-microglobulin: The crucial role of fibrillar seeds. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 291(18), 9678-9689 [10.1074/jbc.M116.720573]. Dettaglio

  • Konijnenberg, A., Ranica, S., Narkiewicz, J., Legname, G., Grandori, R., Sobott, F., et al. (2016). Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein. ANALYTICAL CHEMISTRY, 88(17), 8468-8475 [10.1021/acs.analchem.6b00731]. Dettaglio

  • Ami, D., Lavatelli, F., Rognoni, P., Palladini, G., Raimondi, S., Giorgetti, S., et al. (2016). In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study. SCIENTIFIC REPORTS, 6 [10.1038/srep29096]. Dettaglio

  • Ami, D., Mereghetti, P., Foli, A., Tasaki, M., Milani, P., Nuvolone, M., et al. (2019). ATR-FTIR spectroscopy supported by multivariate analysis for the characterization of adipose tissue aspirates from patients affected by systemic amyloidosis. ANALYTICAL CHEMISTRY, 91(4), 2894-2900 [10.1021/acs.analchem.8b05008]. Dettaglio

  • Tedeschi, G., Mangiagalli, M., Chmielewska, S., Lotti, M., Natalello, A., Brocca, S. (2017). Aggregation properties of a disordered protein are tunable by pH and depend on its net charge per residue. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1861(11), 2543-2550 [10.1016/j.bbagen.2017.09.002]. Dettaglio

Progetti di ricerca

RITESSERE. Silk Sericin materials from textile industry by-products
Anno: 2023
Enti finanziatori: FONDAZIONE CARIPLO
NATALELLO-Fondo per il finanziamento delle attività base di ricerca
Anno: 2017
Bando: FFABR 2017
Enti finanziatori: M.I.U.R. - MINISTERO DELL'ISTRUZIONE, DELL'UNIVERSITA' E DELLA RICERCA - UFFICIO I - Bilancio e Contabilita'. Coordinamento staff della Direzione
Structure-function relation of amyloid: understanding the molecular bases of protein misfolding diseases to design new treatments
Anno: 2013
Bando: 2013-007 - Ricerca Scientifica in ambito biomedico, Ricerca scientifica in ambito biomedico
Enti finanziatori: FONDAZIONE CARIPLO

Premi e responsabilità scientifiche

Premi

  • Inside front cover: Chemical Science, Volume 8, Number 10, October 2017, Chemical Science, the Royal Society of Chemistry., 2017

Incarichi di insegnamento o ricerca

  • Ricercatore universitario a t.d. - Università degli Studi di MILANO-BICOCCA, 2015 - 2018