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@ARTICLE{Lenton:1035302,
      author       = {Lenton, Samuel and Chaaban, Hussein and Khaled, Mohammed
                      and van de Weert, Marco and Strodel, Birgit and Foderà,
                      Vito},
      title        = {{I}nsulin amyloid morphology is encoded in {H}-bonds and
                      electrostatics interactions ruling protein phase separation},
      journal      = {Journal of colloid and interface science},
      volume       = {683},
      issn         = {0021-9797},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2025-00360},
      pages        = {1175 - 1187},
      year         = {2025},
      abstract     = {Ion-protein interactions regulate biological processes and
                      are the basis of key strategies of modulating protein phase
                      diagrams and stability in drug development. Here, 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, circular dichroism and
                      atomistic molecular dynamics (MD) simulations, we found that
                      anions specifically interacting with insulin induced phase
                      separation by neutralising the protein charge and forming
                      H-bond bridges between insulin molecules. The same
                      interaction was responsible for an enhanced insulin
                      conformational stability and resistance to oligomerisation.
                      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, giving rise
                      to elongated amyloid-like fibrils and occurs in the absence
                      of preferential ion-protein binding. Our findings depict a
                      unifying scenario in which common interactions dictated both
                      phase separation at low temperatures and the occurrence of
                      pronounced heterogeneity in the amyloid morphology at high
                      temperatures, similar to what has previously been reported
                      for protein crystal growth.},
      cin          = {IBI-7},
      ddc          = {540},
      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)16},
      pubmed       = {39778472},
      UT           = {WOS:001407781400001},
      doi          = {10.1016/j.jcis.2024.12.058},
      url          = {https://juser.fz-juelich.de/record/1035302},
}