Università della Svizzera italiana

Conformational dynamics and stability of U-shaped and S-shaped amyloid β assemblies

Grasso, Gianvito ; Rebella, Martina ; Muscat, Stefano ; Morbiducci, Umberto ; Tuszynski, Jack ; Danani, Andrea ; Deriu, Marco A.

In: International journal of molecular sciences, 2018, vol. 19, no. 2, p. 571

Alzheimer’s disease is the most fatal neurodegenerative disorder characterized by the aggregation and deposition of Amyloid β (Aβ) oligomers in the brain of patients. Two principal variants of Aβ exist in humans: Aβ1–40 and Aβ1–42. The former is the most abundant in the plaques, while the latter is the most toxic species and forms fibrils more rapidly. Interestingly, fibrils of...

Università della Svizzera italiana

Insights into the effect of the G245S single point mutation on the structure of p53 and the binding of the protein to DNA

Lepre, Marco Gaetano ; Omar, Sara Ibrahim ; Grasso, Gianvito ; Morbiducci, Umberto ; Deriu, Marco Agostino ; Tuszynski, Jack A.

In: Molecules, 2017, vol. 22, no. 8, p. 1358

The transcription factor p53 is a potent tumor suppressor dubbed as the “guardian of the genome” because of its ability to orchestrate protective biological outputs in response to a variety of oncogenic stresses. Mutation and thus inactivation of p53 can be found in 50% of human tumors. The majority are missense mutations located in the DNA binding region. Among them, G245S is known to be...

Università della Svizzera italiana

Modelling protein-protein interactions to elucidate molecular mechanisms behind neurodegenerative diseases

Grasso, Gianvito ; Krause, Rolf (Dir.) ; Danani, Andrea (Codir.)

Thèse de doctorat : Università della Svizzera italiana, 2018 ; 2018INFO017.

The worldwide significant increase in life expectancy has recently drawn the attention of the scientific community to neurodegenerative pathologies of the elderly population. These neurodegenerative disorders arise from the abnormal protein aggregation in the nervous tissue leading to intracellular inclusions or extracellular aggregates in specific brain areas. A feasible strategy to prevent...

Università della Svizzera italiana

Protein environment : a crucial triggering factor in Josephin domain aggregation : the role of 2,2,2-trifluoroethanol

Visentin, Cristina ; Navarro, Susanna ; Grasso, Gianvito ; Regonesi, Maria Elena ; Deriu, Marco Agostino ; Tortora, Paolo ; Ventura, Salvador

In: International journal of molecular sciences, 2018, vol. 19, no. 8, p. 2151

The protein ataxin-3 contains a polyglutamine stretch that triggers amyloid aggregation when it is expanded beyond a critical threshold. This results in the onset of the spinocerebellar ataxia type 3. The protein consists of the globular N-terminal Josephin domain and a disordered C-terminal tail where the polyglutamine stretch is located. Expanded ataxin-3 aggregates via a two-stage...