Methylene blue inhibits nucleation and elongation of SOD1 amyloid fibrils.
作者： Greta Musteikyte , Mantas Ziaunys , Vytautas Smirnovas , None
DOI: 10.7717/PEERJ.9719
关键词: Amyloid 、 Biophysics 、 Superoxide dismutase 、 Chemistry 、 Protein folding 、 Phenothiazine 、 Methylene blue 、 Fibril 、 SOD1 、 Protein aggregation
摘要: Protein aggregation into highly-structured amyloid fibrils is linked to several neurodegenerative diseases. Such fibril formation by superoxide dismutase I (SOD1) considered be related amyotrophic lateral sclerosis, a late-onset and fatal disorder. Despite much effort the discovery of numerous anti-amyloid compounds, no effective cure or treatment currently available. Methylene blue (MB), phenothiazine dye, has been shown modulate multiple amyloidogenic proteins. In this work we show its ability inhibit both spontaneous SOD1 as well elongation preformed fibrils.
peerj.com
sci-hub.st 参考文章(55)
Rosamond Lougheed, John Turnbull, Lack of Effect of Methylene Blue in the SOD1 G93A Mouse Model of Amyotrophic Lateral Sclerosis PLoS ONE. ,vol. 6, pp. e23141- ,(2011) , 10.1371/JOURNAL.PONE.0023141
Yoshiaki Furukawa, Andrew S Torres, Thomas V O'Halloran, Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS The EMBO Journal. ,vol. 23, pp. 2872- 2881 ,(2004) , 10.1038/SJ.EMBOJ.7600276
Lucia Banci, Ivano Bertini, Olga Blaževitš, Vito Calderone, Francesca Cantini, Jiafei Mao, Angela Trapananti, Miguela Vieru, Ilaria Amori, Mauro Cozzolino, Maria Teresa Carrì, Interaction of Cisplatin with Human Superoxide Dismutase Journal of the American Chemical Society. ,vol. 134, pp. 7009- 7014 ,(2012) , 10.1021/JA211591N
Andreas Barth, Infrared spectroscopy of proteins. Biochimica et Biophysica Acta. ,vol. 1767, pp. 1073- 1101 ,(2007) , 10.1016/J.BBABIO.2007.06.004
Alexandra Vaccaro, Shunmoogum A. Patten, Sorana Ciura, Claudia Maios, Martine Therrien, Pierre Drapeau, Edor Kabashi, J. Alex Parker, Methylene Blue Protects against TDP-43 and FUS Neuronal Toxicity in C. elegans and D. rerio PLoS ONE. ,vol. 7, pp. e42117- ,(2012) , 10.1371/JOURNAL.PONE.0042117
Richard J. Nowak, Gregory D. Cuny, Sungwoon Choi, Peter T. Lansbury, Soumya S. Ray, Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods. Journal of Medicinal Chemistry. ,vol. 53, pp. 2709- 2718 ,(2010) , 10.1021/JM901062P
Yoshiaki Furukawa, Thomas V. O'Halloran, Amyotrophic Lateral Sclerosis Mutations Have the Greatest Destabilizing Effect on the Apo- and Reduced Form of SOD1, Leading to Unfolding and Oxidative Aggregation Journal of Biological Chemistry. ,vol. 280, pp. 17266- 17274 ,(2005) , 10.1074/JBC.M500482200
Melissa S. Rotunno, Daryl A. Bosco, An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis Frontiers in Cellular Neuroscience. ,vol. 7, pp. 253- 253 ,(2013) , 10.3389/FNCEL.2013.00253
Gareth S.A. Wright, Svetlana V. Antonyuk, Neil M. Kershaw, Richard W. Strange, S Samar Hasnain, Ligand Binding and Aggregation of Pathogenic Sod1. Nature Communications. ,vol. 4, pp. 1758- 1758 ,(2013) , 10.1038/NCOMMS2750
Robert G Miller, J D Mitchell, Dan H Moore, Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND) Cochrane Database of Systematic Reviews. ,vol. 4, pp. 191- 206 ,(2012) , 10.1002/14651858.CD001447.PUB3