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@ARTICLE{Perez:872764,
      author       = {Perez, Carlos and Miti, Tatiana and Hasecke, Filip and
                      Meisl, Georg and Hoyer, Wolfgang and Muschol, Martin and
                      Ullah, Ghanim},
      title        = {{M}echanism of {F}ibril and {S}oluble {O}ligomer
                      {F}ormation in {A}myloid {B}eta and {H}en {E}gg {W}hite
                      {L}ysozyme {P}roteins},
      journal      = {The journal of physical chemistry / B B, Condensed matter,
                      materials, surfaces, interfaces $\&$ biophysical},
      volume       = {123},
      number       = {27},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2020-00242},
      pages        = {5678 - 5689},
      year         = {2019},
      abstract     = {Assembly and deposition of insoluble amyloid fibrils with a
                      distinctive cross-β-sheet structure is the molecular
                      hallmark of amyloidogenic diseases affecting the central
                      nervous system as well as non-neuropathic amyloidosis.
                      Amyloidogenic proteins form aggregates via kinetic pathways
                      dictated by initial solution conditions. Often, early stage,
                      cytotoxic, small globular amyloid oligomers (gOs) and
                      curvilinear fibrils (CFs) precede the formation of
                      late-stage rigid fibrils (RFs). Growing experimental
                      evidence suggests that soluble gOs are off-pathway
                      aggregates that do not directly convert into the final stage
                      RFs. Yet, the kinetics of RFs aggregation under conditions
                      that either promote or suppress the growth of gOs remain
                      incompletely understood. Here we present a self-assembly
                      model for amyloid fibril formation in the presence and
                      absence of early stage off-pathway aggregates, driven by our
                      experimental results on hen egg white lysozyme (HewL) and
                      beta amyloid (Aβ) aggregation. The model reproduces a range
                      of experimental observations including the sharp boundary in
                      the protein concentration above which the self-assembly of
                      gOs occurs. This is possible when both primary and secondary
                      RFs nucleation rates are allowed to have a nonlinear
                      dependence on initial protein concentration, hinting toward
                      more complex prenucleation and RFs assembly scenarios.
                      Moreover, analysis of RFs lag period in the presence and
                      absence of gOs indicates that these off-pathway aggregates
                      have an inhibitory effect on RFs nucleation. Finally, we
                      incorporate the effect of an Aβ binding protein on the
                      aggregation process in the model that allows us to identify
                      the most suitable solution conditions for suppressing gOs
                      and RFs formation.},
      cin          = {ICS-6},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31246474},
      UT           = {WOS:000475540400002},
      doi          = {10.1021/acs.jpcb.9b02338},
      url          = {https://juser.fz-juelich.de/record/872764},
}