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Overview | Research directions | Group members | Collaborations | Selected Publications


Work in our laboratory covers a wide spectrum of topics related to prions and amyloids, across physiology and disease. We investigate these phenomena by integrating a variety of computational, chemical, biophysical, biochemical and cellular technologies, with the ultimate objective of defining novel therapeutic approaches for neurodegenerative diseases.

Research directions

We are currently focused on two main lines of investigation:

Define new interdisciplinary approaches to study protein misfolding
Aging is intrinsically linked to a broad range of molecular, cellular and functional changes, which particularly affect the integrity of the nervous system. One fundamental process altered by aging is protein folding. When proteins misfold, they acquire alternative conformations capable of seeding a cascade of molecular events, ultimately resulting in neuronal dysfunction and death. Indeed, a wide range of age-related disorders is linked to the accumulation in the brain of insoluble protein aggregates, often called amyloids. Examples include common disorders such as Parkinson’s and Alzheimer’s disease, as well as rarer disorders such as Amyotrophic lateral sclerosis and prion diseases. The latter are among the most unusual and fascinating pathologies linked to protein misfolding, and are caused by the conformational conversion of the cellular prion protein (PrPC), an endogenous cell-surface glycoprotein, into a misfolded isoform, called PrPSc, that accumulates in the central nervous system of affected individuals. PrPSc is an infectious protein (prion), lacking information-coding nucleic acids, which replicates by directly binding to PrPC, and templating its conformational rearrangement into new PrPSc molecules. Our lab is developing highly interdisciplinary computational and experimental schemes to study protein misfolding in a completely new fashion. These integrative approaches are unrevealing unexpected principles underlying protein misfolding and templated-conversion of proteins, inspiring completely novel approaches to tackle related disorders.
















Develop new drug discovery paradigms for neurodegenerative disorders.
Enormous efforts have been expended by academic laboratories and pharmaceutical companies worldwide to understand the key pathogenic events that lye at the root of neurodegenerative diseases. Association studies are drawing unexpected correlations between different neurodegenerative diseases, and suggesting that the pathological processes underlying these disorders may converge on few molecular hubs. We believe that PrPC is one of such factors, by acting as a transducer of neurotoxicity for various pathogenic protein aggregates, including its own misfolded state (PrPSc), as well as toxic oligomers of the amyloid beta (Aβ) peptide, which are associated with Alzheimer’s disease. Following this rationale, our lab is exploring novel cross-disciplinary paradigms to suppress the expression of PrPC and stop its toxicity-transducing activity.

See also Dulbecco Telethon Institute, Lab Biasini @: http://www.telethon.it/en/what-we-do/our-method/institutes/dti

Group members

  • Emiliano Biasini, PI
  • Tania Massignan, postdoctoral Fellow
  • Silvia Biggi, PhD student
  • Giovanni Spagnolli, PhD student
  • Luca Teruzzi, QCB Master student


  • Pietro Faccioli, University of Trento, ITALY
  • Maria Letizia Barreca & Giuseppe Manfroni, University of Perugia, ITALY
  • Romolo Nonno, Istituto Superiore di Sanità, ITALY
  • Jesús R. Requena, University of Santiago de Compostela, SPAIN
  • Joaquin Castilla, CIC-Biogun, SPAIN
  • Ina Vorberg, DZNE, Germany
  • Steven J. Collins, University of Melbourne, Australia
  • Valentina Bonetto, Mario Negri Institute for Pharmacological Research in Milan, ITALY

Selected publications

Biggi S, Pancher M, Stincardini C, Luotti S, Massignan T, Dalle Vedove A, Astolfi A, Gatto P, Lolli G, Barreca ML, Bonetto V, Adami V and Biasini E. Identification of compounds inhibiting prion replication and toxicity by removing PrPC from the cell surface. J Neurochem. In Press (2019)

Spagnolli G, Rigoli M, Orioli S, Sevillano AM, Faccioli P, Wille H, Biasini E & Requena JR. Full atomistic model of prion structure and conversion. PLOS Pathogens. In Press (2019)
Preprint @ https://www.biorxiv.org/content/biorxiv/early/2018/12/22/505271.full.pdf

Rigoli M, Spagnolli G, Faccioli P, Requena JR & Biasini E. Ok Google, how could I design therapeutics against prion diseases? Curr Opin Pharmacol. 2019 May 3;44:39-45. doi: 10.1016/j.coph.2019.03.015.

Biasini E. A designer chaperone against prion diseases. Nat Biomed Eng. 2019 Mar;3(3):167-168. doi: 10.1038/s41551-019-0367-6.

Barreca ML, Iraci N, Biggi S, Cecchetti V, Biasini E. Pharmacological Agents Targeting the Cellular Prion Protein. Pathogens. 2018 Mar 7;7(1). pii: E27. doi: 10.3390/pathogens7010027.

Massignan T, Sangiovanni V, Biggi S, Stincardini C, Elezgarai SR, Maietta G, Andreev IA, Ratmanova NK, Belov DS, Lukyanenko ER, Belov GM, Barreca ML, Altieri A, Kurkin AV, Biasini E. A novel small molecule inhibitor of prion replication and mutant prion protein toxicity. ChemMedChem. 2017 Jul 19. doi: 10.1002/cmdc.201700302.

Elezgarai SR, Biasini E. Common therapeutic strategies for prion and Alzheimer's diseases. Biol Chem. 2016 Nov 1;397(11):1115-1124. doi: 10.1515/hsz-2016-0190.

Massignan T, Cimini S, Stincardini C, Cerovic M, Vanni I, Elezgarai SR, Moreno J, Stravalaci M, Negro A, Sangiovanni V, Restelli E, Riccardi G, Gobbi M, Castilla J, Borsello T, Nonno R, Biasini E. A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein. Sci Rep. 2016 Mar 15;6:23180. doi: 10.1038/srep23180.

Biasini E, Unterberger U, Solomon IH, Massignan T, Senatore A, Bian H, Voigtlaender T, Bowman FP, Bonetto V, Chiesa R, Luebke J, Toselli P and Harris DA. A mutant prion protein sensitizes neurons to glutamate-induced excitotoxicity. J Neurosci. 2013 Feb 6;33(6):2408-18.

Biasini E, Turnbaugh JA, Massignan T, Veglianese P, Forloni G, Bonetto V, Chiesa R and Harris DA. The toxicity of a mutant prion protein is cell-autonomous, and can be suppressed by wild-type prion protein on adjacent cells. PLoS One 2012. 2012;7(3):e33472.

Biasini E, Turnbaugh JA, Unterberger U, Harris DA. Prion protein at the crossroads of physiology and disease. Trends Neurosci. 2012 Feb;35(2):92-103.


For a complete list: https://www.ncbi.nlm.nih.gov/pubmed/?term=emiliano+biasini