Alpha-synuclein structure, functions, and interactions

alpha?synuclein structure, functions, and interactions

at present, when a clinical diagnosis of parkinson’s disease (pd) is made, serious damage has already been done to nerve cells of the substantia nigra pars compacta. the diagnosis of pd in its earlier stages, before this irreversible damage, would be of enormous benefit for future treatment strategies designed to slow or halt the progression of this disease that possibly prevents accumulation o...

Calcium: Alpha-Synuclein Interactions in Alpha-Synucleinopathies

Aggregation of the pre-synaptic protein, α-synuclein (α-syn), is the key etiological factor in Parkinson's disease (PD) and other alpha-synucleinopathies, such as multiple system atrophy (MSA) and Dementia with Lewy bodies (DLB). Various triggers for pathological α-syn aggregation have been elucidated, including post-translational modifications, oxidative stress, and binding of metal ions, such...

Alpha-Synuclein Interactions with Membranes

Synucleinopathies are a group of neurodegenerative disorders that share common pathological intracellular deposits that contain aggregates of the protein ┙-synuclein. Substantial evidence suggests that fibril formation by ┙-synuclein is a critical step in the development of Parkinson's disease (PD). Indeed, in vitro, ┙-synuclein forms fibrils with morphologies and staining characteristics simil...

Alpha-synuclein structure, aggregation and modulators

Effect of Spermidine on Misfolding and Interactions of Alpha-Synuclein

Alpha-synuclein (α-Syn) is a 140 aa presynaptic protein which belongs to a group of natively unfolded proteins that are unstructured in aqueous solutions. The aggregation rate of α-Syn is accelerated in the presence of physiological levels of cellular polyamines. Here we applied single molecule AFM force spectroscopy to characterize the effect of spermidine on the very first stages of α-Syn agg...