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@MISC{Rayan:282945,
      author       = {Rayan, Bader and Barnea, Eilon and Indig, Rinat and
                      Pantoja, Christian Felipe and Gayk, Jesse and Lupu-Haber,
                      Yael and Upcher, Alexander and Argoetti, Amir and Larsen,
                      Jacob and Buell, Alexander and Zweckstetter, Markus and
                      Landau, Meytal},
      title        = {{D}ataset: {RNA} {S}electively {M}odulates {A}ctivity of
                      {V}irulent {A}myloid {PSM}α3 and {H}ost {D}efense {LL}-37
                      via {P}hase {S}eparation and {A}ggregation {D}ynamics, v2},
      publisher    = {Zenodo},
      reportid     = {DZNE-2025-01406},
      year         = {2025},
      abstract     = {Amyloids, classically linked to neurodegenerative diseases,
                      also play critical roles in infection and immunity.
                      Phenol-soluble modulins (PSMs) from Staphylococcus aureus
                      are virulent amyloids that contribute to cytotoxicity,
                      immune modulation, and biofilm stability. PSMα3 forms
                      cross-α amyloid fibrils and shares sequence and structural
                      features with LL-37, a human host-defense peptide that
                      assembles into α-helical structures. Here, we uncover RNA
                      as a potent, context-dependent modulator of their
                      aggregation and activity. RNA consistently reduces LL-37’s
                      cytotoxicity toward human cells without compromising its
                      antibacterial function, suggesting a selective
                      host-protective mechanism. In contrast, RNA preserves
                      PSMα3’s cytotoxic and antimicrobial activity over time,
                      likely by promoting liquid–liquid phase separation (LLPS)
                      and stabilizing bioactive fibrillar polymorphs, enabling S.
                      aureus to fine-tune its virulence strategies. At higher
                      concentrations, RNA drives both peptides toward distinct
                      aggregated states, amorphous for LL-37 and fibrillar for
                      PSMα3, underlying their divergent functional outcomes. The
                      amyloid inhibitor EGCG abolishes the bioactivity of both
                      PSMα3 and LL-37, overriding RNA’s modulatory effects.
                      Together, our findings establish RNA as a key modulator of
                      both virulent amyloids and host-defense peptides, with broad
                      implications for microbial immune evasion, innate immunity,
                      and amyloid-associated diseases. Moreover, they highlight
                      phase transitions as a tunable mechanism for regulating
                      peptide bioactivity and a promising therapeutic target
                      across infectious and neurodegenerative conditions.},
      cin          = {AG Zweckstetter},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)32},
      doi          = {10.5281/zenodo.17116616},
      url          = {https://pub.dzne.de/record/282945},
}