Studeringen av heterologa interaktioner av amyloidproteiner som utlösande faktorer för Parkinsons sjukdom

Abnormal accumulation and aggregation of misfolded α-synuclein (α-syn) are the key pathological processes of Parkinson’s disease (PD), however, it is still unclear how, where and what triggers α-syn aggregation. Our recent studies show that diabetes related Islet amyloid polypeptide (IAPP), bacterial infection related amyloid protein phenol soluble modulins α (PSMα) and aggregated Tau can facilitate α-syn aggregation. Here, we hypothesize that the “heterologous amyloid protein cross-seeding” can induce α-syn nucleation and aggregation at the initial phase of PD.

Using cell-free, cell and animal models, we will employ interdisciplinary methods of biochemistry, molecular biology and biophysical imaging (Soft X-ray spectromicroscopy and label-free optical photothermal infrared super resolution microspectroscopy) to reveal the triggering factors and mechanisms of heterologous amyloid protein cross-seeded α-syn aggregation.