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Accelerated Fibrillation of α-Synuclein Induced by the Combined Action of Macromolecular Crowding and Factors Inducing Partial Folding

[ Vol. 6 , Issue. 3 ]

Author(s):

L. A. Munishkina, A. L. Fink and V. N. Uversky   Pages 252 - 260 ( 9 )

Abstract:


To better model the characteristics of crowded intracellular environments, we examined the effect of several factors known to induce partial folding and accelerated fibrillation of α-synuclein in dilute solutions, on the fibrillation of this protein in a crowded milieu. We found that low pH, certain metals and pesticides, polyanions, polycations and low concentrations of organic solvents cause a significant acceleration of α-synuclein fibrillation in the presence of high concentrations of polyethylene glycol. This suggests that the fibril-promoting effects of factors inducing partial folding of α- synuclein and the fibril-stimulating effects of macromolecular crowding are relatively independent and thus might act additively or even synergistically.

Keywords:

Parkinson's disease, -synuclein, crowding, fibrillation, aggregation, metals, pesticides, organic solvent, polycations, GAGs

Affiliation:

Center for Computational Biology and Bioinformatics, Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 410 W. 10th Street, HS 5009, Indianapolis, IN 46202, USA.



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