ABSTRACT
Introduction ............................................................................................................ 169 (Non)-Specific Interactions of α-Synuclein with Metal Ions ................................ 171 Aluminum .............................................................................................................. 174 Calcium .................................................................................................................. 175 Cobalt ..................................................................................................................... 177 Copper .................................................................................................................... 177 Iron ......................................................................................................................... 179 Magnesium ............................................................................................................. 182 Manganese ............................................................................................................. 183 Terbium .................................................................................................................. 184 Zinc ........................................................................................................................ 184 Future Perspective .................................................................................................. 185 References .............................................................................................................. 185
detected with antibodies to α-synuclein correlate with dementia in PD, DLB, and LBVAD; antibodies to α-synuclein detect LBs in familial AD, sporadic AD, and elderly Down syndrome brains; α-synuclein is a building block of glial cytoplasmic inclusions (GCIs) in neurodegeneration with brain iron accumulation type 1, and multiple system atrophy (MSA); cells transfected with α-synuclein and treated with nitric oxide generators develop LB-like α-synuclein inclusions; biogenic mice overexpress mutant human amyloid precursor protein; and α-synuclein show an augmentation in α-synuclein inclusions. Thus many neurodegenerative diseases are characterized by α-synuclein pathologies resulting from deposition of α-synuclein lesions. The underlying cause of aggregation may result from structural alterations in α-synuclein, an intrinsically disordered protein (IDP) that normally possesses little or no ordered structure under the physiological conditions in vitro (Weinreb et al. 1996; Uversky, Li, and Fink 2001a; Bussell and Eliezer 2001; Eliezer et al. 2001; Uversky 2003, 2007, 2008).
