Oct 1, 2020 · This study illustrates specific effects of metal coordination, and the associated electrostatic charge patterns, on the complex structural space of the intrinsically disordered protein...

Jul 12, 2006 · We recently showed that Cu (II) binds at the N-terminus of AS with high affinity (Kd ∼ 0.1 μM) and accelerates its fibrillation. In this work we investigated the binding features of the divalent metal ions Fe (II), Mn (II), Co (II), and Ni (II), and their effects on AS aggregation.

α-synuclein profiles as an important metal-binding protein in the brain, displaying three main anchoring sites for metal ions with distinct specificity and affinity features. Among all the AS-metal interactions described thus far, the two most physiologically relevant interactions occur with copper and calcium ions.

In this paper, we sought to map the interactions between the di- and trivalent cations, Cu (II), Pb (II), Fe (II), and Fe (III), and the C-terminal region of α-syn encompassing residues 107–140 and to determine how phosphorylation at S129 or Y125 alters the specificity and binding affinity of metals using electrospray ionization-mass spectrometr...

The most recent literature on the interaction between alpha-synuclein in its several aggregation states and metal ions is discussed. This analysis shows two major types of interactions.

Metal ions have been considered as the important etiological factors in PD since their interactions with α-Syn alter the kinetics of fibrillation. In the present study, we have systematically explored the effects of Zn 2+, Cu 2+, Ca 2+, and Mg 2+ cations on α-Syn fibril formation.

Alpha-synuclein has long been studied due to its involvement in the progression of Parkinson's disease (PD), a common neurodegenerative disorder, although a consensus on the exact function of this protein is elusive.

Jan 28, 2015 · Here we give a brief overview on αSyn pathology and the role of metals in the brain and then address in more detail the interaction of αSyn with three disease-relevant transition metals, iron (Fe), copper (Cu) and manganese (Mn).

Feb 3, 2016 · The study of the interaction between divalent and trivalent metal ions with α-synuclein is of vital importance to realize the mechanism of α-synuclein fibrillation. Here we used nuclear magnetic resonance spectroscopy to determine the trivalent metal ions (lanthanides) binding sites in α-synuclein.

Aug 2, 2006 · The aggregation of alpha-synuclein (AS) is characteristic of Parkinson's disease and other neurodegenerative synucleinopathies. Interactions with metal ions affect dramatically the kinetics of fibrillation of AS in vitro and are proposed to play a potential role in vivo.