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@ARTICLE{Intze:279351,
      author       = {Intze, Antonia and Temperini, Maria Eleonora and Rupert,
                      Jakob and Polito, Raffaella and Veber, Alexander and Puskar,
                      Ljiljana and Schade, Ulrich and Ortolani, Michele and Zacco,
                      Elsa and Tartaglia, Gian Gaetano and Giliberti, Valeria},
      title        = {{E}ffect of {RNA} on the supramolecular architecture of
                      α-synuclein fibrils.},
      journal      = {Biophysical journal},
      volume       = {124},
      number       = {12},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {DZNE-2025-00728},
      pages        = {2005 - 2019},
      year         = {2025},
      abstract     = {Structural changes associated with protein aggregation are
                      challenging to study, requiring the combination of
                      experimental techniques providing insights at the molecular
                      level across diverse scales, ranging from nanometers to
                      microns. Understanding these changes is even more complex
                      when aggregation occurs in the presence of molecular
                      cofactors such as nucleic acids and when the resulting
                      aggregates are highly polymorphic. Infrared (IR)
                      spectroscopy is a powerful tool for studying protein
                      aggregates since it combines the label-free sensitivity to
                      the cross-β architecture, an inherent feature of protein
                      supramolecular aggregates, with the possibility to reach
                      nanoscale sensitivity by leveraging atomic force microscopy
                      (AFM)-assisted detection. Here, we present a combined
                      approach that detects IR spectral markers of aggregation
                      using various IR spectroscopy techniques, covering
                      micro-to-nanoscale ranges, to study the effect of RNA on the
                      supramolecular architecture of α-synuclein amyloid
                      aggregates. We show a clear impact of RNA consistent with
                      enhanced intermolecular forces, likely via a stronger
                      hydrogen-bonded network stabilizing the cross-β
                      architecture. AFM-assisted IR spectroscopy was crucial to
                      assess that the more ordered the aggregates are, the
                      stronger the structural impact of RNA. In addition, an
                      RNA-induced reduction of the degree of polymorphism within
                      the aggregate population is obtained.},
      keywords     = {alpha-Synuclein: chemistry / alpha-Synuclein: metabolism /
                      RNA: chemistry / RNA: metabolism / Protein Aggregates /
                      Amyloid: chemistry / Microscopy, Atomic Force /
                      Spectrophotometry, Infrared / Humans / alpha-Synuclein (NLM
                      Chemicals) / RNA (NLM Chemicals) / Protein Aggregates (NLM
                      Chemicals) / Amyloid (NLM Chemicals)},
      cin          = {AG Milovanovic (Bonn)},
      ddc          = {570},
      cid          = {I:(DE-2719)1013043},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40329536},
      doi          = {10.1016/j.bpj.2025.04.031},
      url          = {https://pub.dzne.de/record/279351},
}