Next Article in Journal
Isolation, NMR Spectral Analysis and Hydrolysis Studies of a Hepta Pyranosyl Diterpene Glycoside from Stevia rebaudiana Bertoni
Next Article in Special Issue
Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase
Previous Article in Journal
Quantum Mechanical Modeling: A Tool for the Understanding of Enzyme Reactions
Article Menu

Export Article

Open AccessArticle
Biomolecules 2013, 3(3), 703-732;

Biophysical Characterization of α-Synuclein and Rotenone Interaction

Department of Chemistry and Biochemistry, University of California, 156 High Street, Santa Cruz, CA 95064, USA
Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida; 12901 Bruce B. Downs Blvd., MDC 7, Tampa, FL 33612, USA
Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino 142292, Moscow Region, Russia
Author to whom correspondence should be addressed.
This article is dedicated to Prof. Anthony L. Fink.
Received: 13 September 2013 / Revised: 21 September 2013 / Accepted: 23 September 2013 / Published: 24 September 2013
(This article belongs to the Special Issue Protein Folding and Misfolding)
PDF [1349 KB, uploaded 24 September 2013]


Previous studies revealed that pesticides interact with α-synuclein and accelerate the rate of fibrillation. These results are consistent with the prevailing hypothesis that the direct interaction of α-synuclein with pesticides is one of many suspected factors leading to α-synuclein fibrillation and ultimately to Parkinson’s disease. In this study, the biophysical properties and fibrillation kinetics of α-synuclein in the presence of rotenone were investigated and, more specifically, the effects of rotenone on the early-stage misfolded forms of α-synuclein were considered. The thioflavine T (ThT) fluorescence assay studies provide evidence that early-phase misfolded α-synuclein forms are affected by rotenone and that the fibrillation process is accelerated. Further characterization by attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR) shows that rotenone increases the amount of ordered secondary structure in this intrinsically disordered protein. Morphological characterization by transmission electron microscopy (TEM) and atomic force microscopy (AFM) provide visualization of the differences in the aggregated α-synuclein species developing during the early kinetics of the fibrillation process in the absence and presence of rotenone. We believe that these data provide useful information for a better understanding of the molecular basis of rotenone-induced misfolding and aggregation of α-synuclein. View Full-Text
Keywords: α-Synuclein; Parkinson’s disease; environmental toxin; misfolding; fibrillation; intrinsically disordered protein; pesticide; agrochemical; rotenone α-Synuclein; Parkinson’s disease; environmental toxin; misfolding; fibrillation; intrinsically disordered protein; pesticide; agrochemical; rotenone

Figure 1

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Share & Cite This Article

MDPI and ACS Style

Silva, B.A.; Einarsdóttir, Ó.; Fink, A.L.; Uversky, V.N. Biophysical Characterization of α-Synuclein and Rotenone Interaction. Biomolecules 2013, 3, 703-732.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top