Molecular processes of polyQ protein aggregation studied with time-resolved ATR-FTIR spectroscopy

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Polyglutamine (polyQ) diseases belong to neurodegenerative disorders caused by expanded glutamine repeats in proteins. One well known case is Chorea Huntington. We have studied the aggregation process with an engineered polyQ protein of the type His-SUMO-N17-PolyQ56-Flag. The construct mimics the natively extended polyglutamine sequence with the flanking N-terminal sequence (N17) of the Huntingtin protein. The SUMO (Small Ubiquiting-like Modifier) part keeps the protein soluble and a protease recognition sequence allows Ulp1 (Ubiquitin-like-specific protease1) cleavage. We analyzed the aggregation process by infrared difference spectroscopy in order to gain insights into the molecular mechanisms and potential intermediates. The overlaying spectral contributions of SUMO and Ulp1 have to be distinguished from the polyQ sequence under study. With a combination of Attenuated Total Reflection (ATR)-FTIR spectroscopy and immobilization approaches we could satisfy the high requirements for a spectroscopic study of amyloid proteins. Our data indicates the aggregation of the glutamine sequence to an amyloid β-sheet with an α-helical N17 part. We could not identify any intermediate states, indicating that the aggregation process is highly cooperative.

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ISO 690YUSHCHENKO, Tetyana, Renate SCHLÖMER, Elke DEUERLING, Karin HAUSER, 2015. Molecular processes of polyQ protein aggregation studied with time-resolved ATR-FTIR spectroscopy. In: European Biophysics Journal. 2015, 44(1 Suppl.), pp. S159. ISSN 0175-7571. eISSN 1432-1017. Available under: doi: 10.1007/s00249-015-1045-6
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@article{Yushchenko2015Molec-32234,
  year={2015},
  doi={10.1007/s00249-015-1045-6},
  title={Molecular processes of polyQ protein aggregation studied with time-resolved ATR-FTIR spectroscopy},
  number={1 Suppl.},
  volume={44},
  issn={0175-7571},
  journal={European Biophysics Journal},
  author={Yushchenko, Tetyana and Schlömer, Renate and Deuerling, Elke and Hauser, Karin},
  note={Posterbeitrag}
}
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    <dcterms:abstract xml:lang="eng">Polyglutamine (polyQ) diseases belong to neurodegenerative disorders caused by expanded glutamine repeats in proteins. One well known case is Chorea Huntington. We have studied the aggregation process with an engineered polyQ protein of the type His-SUMO-N17-PolyQ56-Flag. The construct mimics the natively extended polyglutamine sequence with the flanking N-terminal sequence (N17) of the Huntingtin protein. The SUMO (Small  Ubiquiting-like Modifier) part keeps the protein soluble and a protease recognition sequence  allows  Ulp1  (Ubiquitin-like-specific  protease1) cleavage. We analyzed the aggregation process by infrared difference spectroscopy in order to gain insights into the molecular  mechanisms and potential intermediates. The overlaying spectral contributions of SUMO and Ulp1 have to be distinguished from the polyQ sequence under study. With a combination of Attenuated Total Reflection (ATR)-FTIR spectroscopy and immobilization approaches we could satisfy the high requirements for a spectroscopic study of amyloid proteins. Our data indicates the aggregation of the glutamine sequence to an amyloid β-sheet with an α-helical N17 part. We could not identify any intermediate states, indicating that the aggregation process is highly cooperative.</dcterms:abstract>
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