%0 Journal Article
%T Dopamine cannot promote oligomerization of unoxidized <i>¦Á</i>-synuclein
%A Sakurako Shimotakahara
%A Mika Matsui
%A Chiseko Sakuma
%A Teruaki Takahashi
%A Takashi Fujimoto
%A Kazuo Furihata
%A Masaki Kojima
%A Shohei Seino
%A Tomoya Machinami
%A Yoichi Shibusawa
%A Kenji U¨¦da
%A Mitsuru Tashiro
%J Journal of Biophysical Chemistry
%P 110-114
%@ 2153-0378
%D 2013
%I Scientific Research Publishing
%R 10.4236/jbpc.2013.43015
%X <b><i><span style=\"font-family:'Arial','sans-serif';font-size:10pt;\">¦Á</span></i></b><b><span style=\"font-family:'Arial','sans-serif';font-size:10pt;\">-Synuclein is the major component of the filamentous Lewy bodies and Lewy neurites that define neuropathological features of Parkinson¡¯s disease and dementia with Lewy bodies. To investigate the oligomerization process of <i>¦Á</i>-synuclein in association with dopamine (DA), the structural propensities to form oligomers were studied using NMR and other biophysical techniques. The<sup>1</sup>H-<sup>15</sup>N HSQC spectra indicated that both N- and C-termini interacted with DA. Although interactions with DA were also observed in the presence of glutathione by ESI-MS, the significant suppression of oligomerization was observed in the size exclusion chromatography, suggesting that oxidations of <i>¦Á</i>-synuclein are required for its oligomerization.</span></b><b><span style=\"font-family:'Arial','sans-serif';font-size:10pt;\"></span></b>
%K &lt
%K i&gt
%K ¦Á&lt
%K /i&gt
%K -Synuclein
%K Dopamine
%K Glutathione
%K Oligomerization
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=35687