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@ARTICLE{Lenton:1033770,
      author       = {Lenton, Samuel and Chaaban, Hussein and Khaled, Mohammed
                      and Van de Weert, Marco and Strodel, Birgit and Fodera,
                      Vito},
      title        = {{A}myloid {M}orphology is {E}ncoded in {H}-bonds and
                      {E}lectrostatics {I}nteractions {R}uling {P}rotein {P}hase
                      {S}eparation},
      journal      = {bioRxiv},
      reportid     = {FZJ-2024-06611},
      pages        = {40},
      year         = {2024},
      abstract     = {We report the mechanisms by which H-bonds and electrostatic
                      interactions in ion- protein systems determine phase
                      separation and amyloid formation. Using microscopy,
                      small-angle X-ray scattering and atomistic molecular
                      dynamics simulations, we found that anions interacting with
                      insulin induced phase separation by neutralising the pro-
                      tein charge and forming H-bonds between insulin molecules.
                      The same interaction was responsible for an enhanced insulin
                      conformational stability and resistance to oligomeri-
                      sation. Under aggregation conditions, the anion-protein
                      interaction translated into the activation of a coalescence
                      process, leading to amyloid-like microparticles. This
                      reaction is alternative to conformationally-driven pathways,
                      which give rise to amyloid-like fibrils and core-shell
                      structures, and occur instead in the absence of ion-protein
                      binding. Our findings depict a scenario in which common
                      interactions dictated both phase separation at low
                      temperatures and the occurrence of heterogeneity in the
                      amyloid morphology at high temperatures, similar to what has
                      been reported for protein crystallisation.},
      cin          = {IBI-7},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)25},
      doi          = {10.1101/2024.01.10.574993},
      url          = {https://juser.fz-juelich.de/record/1033770},
}