Modulation of alpha-synuclein aggregation by dopamine analogs (Contributo in atti di convegno)

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  • Modulation of alpha-synuclein aggregation by dopamine analogs (Contributo in atti di convegno) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Alternative label
  • Giuseppe Legname1,2,#, Diane Latawiec1,2, Fernando Herrera2,3, Alpan Bek4, Michela Candotti2,3, Federico Benetti1,2, Vincenzo Grillo5, Elvio Carlino5, Marco Lazzarino4,5, Stefano Gustincich1,2 and Paolo Carloni2,3, (2009)
    Modulation of alpha-synuclein aggregation by dopamine analogs
    in Microscopy Conference 2009, Graz (A), 30 Aug. Sept 4 2009
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Giuseppe Legname1,2,#, Diane Latawiec1,2, Fernando Herrera2,3, Alpan Bek4, Michela Candotti2,3, Federico Benetti1,2, Vincenzo Grillo5, Elvio Carlino5, Marco Lazzarino4,5, Stefano Gustincich1,2 and Paolo Carloni2,3, (literal)
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  • Microscopy Conference 2009 (literal)
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  • 2 (literal)
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  • 1Department of Neurobiology, 2Italian Institute of Technology (IIT)-SISSA Unit, Via Beirut 2-4, 34014 Trieste, Italy.3Department of Statistical and Biological Physics, Scuola Internazionale Superiore di Studi Avanzati-International School for Advanced Studies (SISSA-ISAS), I-34014 Trieste, Italy. 4LANA3DA Scanning Probe BioNanoAnalysis, CBM, I-34012 Trieste-Italy; 5TASC-INFM-CNR National Laboratory, I-34012 Trieste, Italy. (literal)
Titolo
  • Modulation of alpha-synuclein aggregation by dopamine analogs (literal)
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  • Pabst, Zellnig (literal)
Abstract
  • Parkinson's disease is a fatal neurodegenerative movement disorder, which affects an estimated four million people worldwide [1]. However, no known cure exists. The action of dopamine on the aggregation of ?-synuclein (?-syn) is associated with the onset of the pathogenesis of the disease and recent studies have revealed that dopamine and its analogs can inhibit aggregation of ?-syn [2-6]. Here, we have used a combined computational and experimental/microscopical approach to investigate the effect of dopamine mimickers on the aggregation of ?-syn. Using computational methods, small molecules were found in the ligand.info database [7], which are structurally and electrostatically similar to dopamine. Molecular dynamics simulations showed that binding to ?-syn is much weaker than that of dopamine, which inhibits fibrillation [8]. Five of the identified molecules were tested in an in vitro fibrillization assay and analyzed by high-resolution atomic force microscopy (AFM) and transmission electron microscopy (TEM) (literal)
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