Giuseppe GRASSO

Associate Professor of [CHIM/03]
Office: Cittadella Universitaria, V.le A. Doria 6, 95125 Catania. Edificio 1 corpo B piano terra corridoio a destra
Phone: +39 095 738 5046
Office Hours: Monday and Wednesday from 11:00 to 13:00 E' consigliabile contattare il docente via email

Associate Professor in General and Inorganic Chemistry (03/B1). President of the Bachelor of Science in Chemistry.

Courses: General and Inorganic Chemistry (9 CFU) at the B.D. course in Biological Sciences and General and Inorganic Chemistry and laboratory (6 CFU) -Module 2 at the B.D. course in Chemistry

Main research topics:

  1. Metal dishomeostasis in Alzheimer's disease
  2. The role of Insulin-degrading enzyme in Alzheimer's disease
  3. The study of proteosome activity and its modulation Alzheimer's disease e Rett's syndrome
  4. Mass spectrometry applied to the characterisation of functionalised nanoparticles
  5. Bioinorganic Chemistry
  6. Mass Spectrometry and study of biomolecular interactions through Surface Plasmon Resonance

ORCID ID: 0000-0002-7179-4835


He was born in 1977 in Catania and in 2000 obtained the “Laurea” in Chemistry in Catania (110/110 cum laude) from the University of Catania and in 2004 the PhD in Chemistry from the University of Nottingham (UK). After several post-docs in Italy and England, he finally got a permanent position at the University of Catania in 2010 where he is currently employed as an Associate Professor. He obtained the National Scientific Qualification for becoming a Full Professor in “Chemical Sciences and Inorganic Systems” (03/B1) and in Chemical Fundamentals in Technologies (03/B2). He has given several courses to PhD students (course: “ A bioinorganic approach to neurodegenerative diseases”), undergraduate students (courses: “General and Inorganic Chemistry” (9 CFU); Bioinorganic Chemistry (6 CFU)), master students (Modules: A.2.4 – Spectroscopy for Molecular diagnosis 2; A.3.6- Metal complexes as antitumoral drugs and their targets; course: “Microdestructive techniques and laser desorption techniques”).



Giuseppe Grasso has authored or co-authored 69 papers and he has an h-index of 25. He has attended more than 60 international conferences, presenting his work either as an oral communication or as a keynote lecture.

He has been selected for the “Fulbright Visiting Scholar Program” 2015/2016 and spent 9 months at the University of Pennsylvania, working on “Apolipoprotein E, metals and Alzheimer's Disease: uncovering underlying unifying mechanism to explain pathogenesis”.

He has been participating to several funded project and is the PI and national coordinator of a funded PRIN project Prot. 20157WZM8A, entitled: “Role of metal dyshomeostasis and ubiquitin-proteasome system derangement in brain pathologies: risk factors and neuroprotective strategies”.

G. Grasso's publications in the last 5 years


  1. Pyrazolones activate proteasome by gating mechanisms and protect neuronal cells from Aβ amyloid toxicity

A.M. Santoro, V. Lanza, F. Bellia, D. Sbardella, G.R. Tundo, A. Cannizzo, G. Grasso, M. Arizzi, V.G. Nicoletti, S. Alcaro, G. Costa, A. Pietropaolo, G. Malgieri, G. D'Abrosca, R.o Fattorusso, S. García-Viñuales, I.M.M. Ahmed, M. Coletta, D. Milardi

ChemMedChem (2020) 15, 302–316.

  1. The use of mass spectrometry to study Zn-metalloprotease-substrate interactions

G. Grasso

Mass Spectrometry Reviews (2020) 39, 574–585.

  1. Defective proteasome biogenesis into skin fibroblasts isolated from Rett Syndrome subjects with MeCP2 non-sense mutations

D. Sbardella; G.R. Tundo; V. Cunsolo; G. Grasso; R. Cascella; V. Caputo; A.M. Santoro; D. Milardi; A. Pecorelli; C. Ciaccio; D. Di Pierro; S. Leoncini; L. Campagnolo; V. Pironi; F. Oddone; P. Manni; S. Foti; E. Giardina; C. De Felice; Y. Hayek; P. Curatolo; C. Galasso; G. Valacchi; M. Coletta; G. Graziani; S. Marini

BBA - Molecular Basis of Disease (2020) 1866, 165793.

4. The proteasome as a druggable target with multiple therapeutic potentialities: cutting and non-cutting edges

G.R. Tundo, D. Sbardella, A.M. Santoro, A. Coletta, F. Oddone, G. Grasso, D. Milardi, P. Lacal, S. Marini, P. Purrello, G. Graziani, M. Coletta

Pharmacology & Therapeutics (2020) 107579.


1. Amyloid beta proteins modified by PUFA oxidation products in Alzheimer’s disease brain

H.A. Mourelatos, H. Komatsu, R. Furman, G. Grasso, P.H. Axelsen

Biophysical Journal 114(3):229a-230a DOI: 10.1016/j.bpj.2017.11.1277

2. Mass spectrometry is a multifaceted weapon to be used in the battle against Alzheimer’s disease: amyloid beta peptides and beyond

G. Grasso

Mass Spectrometry Reviews (2019) 38, 34–48.

3. Site directed mutagenesis of insulin-degrading enzyme allows singling out the molecular basis of peptidase versus E1-like activity: the role of metal ions

F. Bellia, V. Lanza, I. Mohamed Mohamud Ahmed, S. Garcia-Vinuales, E. Veiss, M. Arizzi, D. Calcagno, D. Milardi, G. Grasso

Metallomics (2019) 11, 278–281.

4. Ubiquitin binds the Amyloid β peptide and interferes with its clearance pathways

F. Bellia, V. Lanza, S. García-Viñuales, I. M. M. Ahmed, A. Pietropaolo, C. Iacobucci, G. Malgieri, G. D’Abrosca, R. Fattorusso, V. G. Nicoletti, D. Sbardella, G. R. Tundo, M. Coletta, D. Calcagno, L. Pirone, E. Pedone, G. Grasso, D. Milardi

Chemical Science (2019) 10, 2732–2742.

5. IDE degrades Nociceptin/Orphanin FQ through an insulin regulated mechanism

G.A. Zingale, F. Bellia, I.M.M. Ahmed, P. Mielczarek, J. Silberring, G. Grasso

International Journal of Molecular Science (2019) 20, 4447–4457.


1. Carnosine protects pancreatic beta cells and islets against oxidative stress damage

V Miceli, M Pampalone, G Frazziano, G Grasso, E Rizzarelli, C Ricordi, A Casu, G Iannolo, PG Conaldi,

Molecular and Cellular Endocrinology (2018)  474, 105–118.

2. "Enzyme Kinetics from Circular Dichroism of Insulin..." by Noel D. Lazo (invited commentary)

G. Grasso

Bioscience Reports (2018) 38, BSR20181555.

3. The insulin degrading enzyme is an allosteric modulator of the 20S proteasome and a potential competitor of the 19S

D. Sbardella, G.R. Tundo, A. Coletta, J. Marcoux, E.I. Koufogeorgou, C. Ciaccio, A.M. Santoro, D. Milardi, G. Grasso, P. Cozza, M.-P. Bousquet-Dubouch, S. Marini, M. Coletta

Cellular and Molecular Life Sciences (2018) 75, 3441–3456.


1.Effects of covalent modification by 4-hydroxy-2-nonenal on the noncovalent oligomerization of ubiquitin

G. Grasso, P.H. Axelsen

Journal of Mass Spectrometry (2017) 52, 36-42.

2. Atmospheric pressure MALDI for the non-invasive characterization of carbonaceous ink from Renaissance documents

G. Grasso, M. Calcagno, A. Rapisarda, R. D’Agata, G. Spoto

Analytical and Bionalytical Chemistry (2017) 409, 3943-3950.

3. Multiple functions of insulin-degrading enzyme: a metabolic crosslight?

G.R. Tundo, D. Sbardella, C. Ciaccio, G. Grasso, M. Gioia, A. Coletta, F. Polticelli, D. Di Pierro, D. Milardi, P. Van Endert, S. Marini, M .Coletta

Critical Reviews in Biochemistry and Molecular Biology (2017) 52, 554–582

4. Inhibition of Aβ amyloid growth and toxicity by silybins: the crucial role of stereochemistry

M. Sciacca, V. Romanucci, A. Zarrelli, I. Monaco, F. Lolicato, N. Spinella, C. Galati, G. Grasso, L. D'Urso, M. Romeo, L. Diomede, M. Salmona, C. Bongiorno, G. Di Fabio, C. La Rosa, D. Milardi

ACS Chemical Neuroscience (2017) 8, 1767–1778.

5. The double faced role of copper in Aβ homeostasis: a survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration

G. Grasso, A.M. Santoro, V. Lanza, D. Sbardella, G.R. Tundo, C. Ciaccio, S. Marini, M. Coletta, D. Milardi

Coordination Chemistry Reviews  (2017) 347, 1–22.

6. Covalent modifications of the amyloid beta peptide by hydroxynonenal: effects on metal ion binding by monomers and insights into the fibril topology

G. Grasso, H. Komatsu, P.H. Axelsen

Journal of Bioinorganic Chemistry (2017) 174, 130–136.

7. Surface tailoring of polyacrylate-grafted graphene oxide for controlled interactions at the biointerface

G. Consiglio, P. Di Pietro, L. D'Urso, G. Forte, G. Grasso, C. Sgarlata, D. Cossement, R. Snyders, C. Satriano

Journal of Colloid & Interface Science (2017) 506, 532–542.

8. Metals are main actors in the biological world

G. Grasso

Metals (2017) 7, 422 (Editorial)


1. Copper, differently from zinc, affects bradykinin conformation, oligomerization state and activity

I. Naletova, V. G. Nicoletti, D. Milardi, A. Pietropaolo, G. Grasso

Metallomics (2016) 8, 750-761.

2. Ubiquitin associates with the N-terminal domain of the Nerve Growth Factor: the role of Cu(II) ions

V. Lanza, A. Travaglia, G. Malgieri, R. Fattorusso, G. Grasso, G. Di Natale, V. Zito, G. Arena, D. Milardi, E. Rizzarelli

Chemistry-A European Journal (2016) 22, 17767-17775.

3. pH sensitive functionalized graphene oxide as a carrier for delivering Gemcitabine: A computational approach

C. Sgarlata, L. D’Urso, G. Consiglio, G. Grasso, C. Satriano, G. Forte

Computational and Theoretical Chemistry (2016) 1096, 1-6.


1. A neglected modulator of insulin-degrading enzyme activity and conformation: the pH

G. Grasso, C. Satriano, D. Milardi

Biophysical Chemistry (2015) 203-204, 33-40.

2. The insulin degrading enzyme activates ubiquitin and promotes the formation of K48 and K63 diubiquitin

G. Grasso, V. Lanza, G. Malgieri, R. Fattorusso, A. Pietropaolo, E. Rizzarelli, D. Milardi

Chemical Communications (2015) 51, 15724-15727.

Insegnamenti tenuti presso altri dipartimenti

The research of Dr. Grasso is focused on the study of molecular interactions between biomolecules involved in certain neurodegenerative diseases such as Alzheimer's disease. In particular, some metalloproteases such as insulin-degrading enzyme (IDE) involved with these diseases are studied and the possibility of modulating the enzymatic activity of these biomolecules for therapeutic purposes is investigated. The influence that metal ions such as copper or zinc and oxidative stress have on the biomolecular mechanisms involved in neurodegeneration is also studied using various analytical techniques such as mass spectrometry, surface plasmon resonance, NMR as well as biochemical methods.

Schematic sketch of the processes in which IDE appears to be involved as a regulator of cell homeostasis: (A) The twofold protective role of IDE in amyloidogenic aggregation: IDE can neutralize amyloidogenic peptides either by a proteolysis-independent “dead-end” chaperone-like activity on both Ab1–42 monomers and a-synuclein (a-Syn) oligomers, or by a degradation of a large number of amyloidogenic substrates, thus preventing further assembly of peptides into toxic aggregates. (B) A working hypothesis of the links between the UPS and IDE. The canonical conjugation pathway for Ub is carried out by a set of three enzymes. Along with ATP, E1 starts the ubiquitination process. Ub is first activated by E1 and subsequently transferred to E2. The E2 protein complexes with E3 which catalyzes the transfer of Ub to the protein. Multiple cycles of binding to charged E2 enzymes lead to the formation of Ub chains, which are recognized by the 26S proteasome, facilitating substrate degradation. IDE can tightly interact with components of the UPS system: IDE can form a complex with Ub, likely acting as E1 enzyme. Moreover, IDE can bind to the outer surface of 20S proteasome, modulating 20S activities and its binding to regulatory particle. (C) Up regulation of IDE in non-malignant and malignant cells under stressful conditions. In several human tumours, a down regulation of IDE expression has been associated with the apoptotic death of the cells. (D) A general scheme of the hypothetical effect of the fluctuation of IDE levels in the regulation of cell viability and homeostasis is depicted (from Critical Reviews in Biochemistry and Molecular Biology (2017).

Giuseppe Grasso has been elected President of the Bachelore of Science in Chemistry (11/2020-10/2024);

he is the coordinator and referent of the ERASMUS exchange between the Department of Chemical Sciences of the University of Catania and the following Universities:


He loves to travel and has lived several years abroad (4 years in UK and 9 months in USA).