@article{Przybylski2010Prote-52627,
  year={2010},
  doi={10.1002/psc.1301},
  title={Proteolytic intermediates in the oligomerisation-aggregation pathway of alpha-synuclein revealed by ion mobility mass spectrometry},
  number={S1},
  volume={16},
  issn={1075-2617},
  journal={Journal of Peptide Science},
  author={Przybylski, Michael and Vlad, Camelia and Lindner, Kathrin and Ciossek, Thomas and Hengerer, Bastian and Leist, Marcel},
  note={Meeting Abstract}
}

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    <dc:contributor>Vlad, Camelia</dc:contributor>
    <dc:contributor>Lindner, Kathrin</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-01-29T12:14:20Z</dcterms:available>
    <dcterms:title>Proteolytic intermediates in the oligomerisation-aggregation pathway of alpha-synuclein revealed by ion mobility mass spectrometry</dcterms:title>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-01-29T12:14:20Z</dc:date>
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    <dc:creator>Ciossek, Thomas</dc:creator>
    <dcterms:issued>2010</dcterms:issued>
    <dc:creator>Przybylski, Michael</dc:creator>
    <dc:language>eng</dc:language>
    <dc:creator>Leist, Marcel</dc:creator>
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    <dc:contributor>Przybylski, Michael</dc:contributor>
    <dc:creator>Lindner, Kathrin</dc:creator>
    <dc:contributor>Ciossek, Thomas</dc:contributor>
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    <dcterms:abstract xml:lang="eng">A variety of diseases, previously thought to be unrelated, such as cancer and neurodegenerative diseases, are characterised by the formation of ”misfolded”protein aggregates. While ”soft-ionisation”mass spectrometry (MS), particularly electrospray-MS (ESI-MS), has substantially contributed to peptide analysis and proteomics, ESI-MS is not suitable to direct ”in-situ”analysis of conformational states and intermediates. Recently, ion mobility mass spectrometry (IM-MS) is emerging as a new tool to probe protein structures and interactions due to its potential for separation polypeptides by conformational states, shape and topology. We report here first applications of IM-MS to the characterization of reaction intermediates in the in vitro oligomerisation and aggregation of alpha-synuclein (αSyn), a key polypeptide in Parkinson’s disease. IM-MS of the in vitro aggregation of wt-αSyn enabled the structure elucidation of several hitherto unknown N- and C-terminal products, and a proteolytic fragment at V71-T72 in the aggregation domain (C-VT72; 7.2 kDa), which appears to be a key intermediate in the aggregation pathway; in vitro studies of this fragment prepared by chemical synthesis and bacterial expression showed a dramatically enhanced rate of aggregation. Most recently, IM-MS was also successfully applied to the direct analysis of affinity-captured αSyn from biological samples, such as brain homogenate, indicating this method as a powerful new tool to the molecular characterization of conformation-dependant intermediates of protein aggregation.</dcterms:abstract>
    <dc:creator>Hengerer, Bastian</dc:creator>
    <dc:creator>Vlad, Camelia</dc:creator>
    <dc:contributor>Hengerer, Bastian</dc:contributor>
    <dc:contributor>Leist, Marcel</dc:contributor>
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