[NMR paper] Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
Related ArticlesTemperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
PLoS One. 2013;8(1):e53487
Authors: Ariesandi W, Chang CF, Chen TE, Chen YR
Abstract
Amyloid fibrils of ?-synuclein are the main constituent of Lewy bodies deposited in substantial nigra of Parkinson's disease brains. ?-Synuclein is an intrinsically disordered protein lacking compact secondary and tertiary structures. To enhance the understanding of its structure and function relationship, we utilized temperature treatment to study ?-synuclein conformational changes and the subsequent effects. We found that after 1 hr of high temperature pretreatment, >80°C, ?-synuclein fibrillization was significantly inhibited. However, the temperature melting coupled with circular dichroism spectra showed that ?-synuclein was fully reversible and the NMR studies showed no observable structural changes of ?-synuclein after 95°C treatment. By using cross-linking and analytical ultracentrifugation, rare amount of pre-existing ?-synuclein oligomers were found to decrease after the high temperature treatment. In addition, a small portion of C-terminal truncation of ?-synuclein also occurred. The reduction of pre-existing oligomers of ?-synuclein may contribute to less seeding effect that retards the kinetics of amyloid fibrillization. Overall, our results showed that the pre-existing oligomeric species is a key factor contributing to ?-synuclein fibrillization. Our results facilitate the understanding of ?-synuclein fibrillization.
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 15;
Authors: Binolfi A, Valiente-Gabioud AA, Duran R, Zweckstetter M, Griesinger C, Fernandez CO
The aggregation of ?-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate...
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Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy
Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy
Andres Binolfi, Ariel A. Valiente-Gabioud, Rosario Duran, Markus Zweckstetter, Christian Griesinger and Claudio O. Fernandez
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107842f/aop/images/medium/ja-2010-07842f_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107842f
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/b4TqLrO3oG4
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[NMR paper] Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble
Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
Related Articles Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
J Am Chem Soc. 2005 Jan 19;127(2):476-7
Authors: Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM
The intrinsically disordered protein alpha-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of alpha-synuclein...
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11-24-2010 11:14 PM
[NMR paper] NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of i
NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.
Related Articles NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.
EMBO J. 2004 May 19;23(10):2039-46
Authors: Fernández CO, Hoyer W, Zweckstetter M, Jares-Erijman EA, Subramaniam V, Griesinger C, Jovin TM
The aggregation of alpha-synuclein is characteristic of Parkinson's disease (PD) and other neurodegenerative synucleinopathies. The 140-aa protein is natively unstructured; thus,...
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11-24-2010 09:51 PM
[NMR paper] Pressure-dependent changes in the structure of the melittin alpha-helix determined by
Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR.
Related Articles Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR.
J Biomol NMR. 2001 Feb;19(2):115-24
Authors: Iwadate M, Asakura T, Dubovskii PV, Yamada H, Akasaka K, Williamson MP
A novel method is described, which uses changes in NMR chemical shifts to characterise the structural change in a protein with pressure. Melittin in methanol is a small alpha-helical protein, and its chemical shifts change linearly...
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11-19-2010 08:32 PM
[NMR paper] Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through
Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
Related Articles Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
J Biol Chem. 1998 Oct 16;273(42):27357-63
Authors: McInnes C, Wang J, Al Moustafa AE, Yansouni C, O'Connor-McCourt M, Sykes BD
The investigation of a...
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[NMR paper] Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in m
Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in monitoring a protein NMR structure refinement.
Related Articles Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in monitoring a protein NMR structure refinement.
J Biomol NMR. 1995 Feb;5(2):161-72
Authors: Celda B, Biamonti C, Arnau MJ, Tejero R, Montelione GT
A large portion of the 13C resonance assignments for murine epidermal growth factor (mEGF) at pH 3.1 and 28 degrees C has been determined at natural isotope abundance....
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08-22-2010 03:41 AM
[NMR paper] Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequen
Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and...
Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
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