Rosaria Rita Arrostuto
Computational investigation of Amyloid Precursor Protein Familial Mutants and their interaction with F-spondin in Alzheimer’s Disease.
Rel. Jacek Adam Tuszynski. Politecnico di Torino, Corso di laurea magistrale in Ingegneria Biomedica, 2025
|
Preview |
PDF (Tesi_di_laurea)
- Tesi
Licenza: Creative Commons Attribution Non-commercial No Derivatives. Download (7MB) | Preview |
Abstract
Alzheimer's disease (AD) is a neurodegenerative disease and represents the most common form of dementia, characterized by a progressive deterioration of memory and cognitive functions. It mainly affects the elderly population (late onset) but can also occur at a younger age (early onset), especially in the presence of genetic mutations. According to the amyloid hypothesis, a central role is played by the amyloid precursor protein (APP), which is cleaved by β- and γ-secretase through the amyloidogenic pathway, generating the Amyloid Beta (Aβ) protein, in particular Aβ42, a form more prone to aggregation and neurotoxic. Familial APP mutations, such as the Swedish (KM670/671NL), Iowa (D694N) and Iberian (I716F) mutations, alter APP processing, favoring the pathological accumulation of Aβ.
A possible strategy to counteract this mechanism is the use of ligands capable of binding to APP and preventing the initial cleavage by β-secretase
Tipo di pubblicazione
URI
![]() |
Modifica (riservato agli operatori) |
