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@ARTICLE{Hasecke:888243,
      author       = {Hasecke, Filip and Niyangoda, Chamani and Borjas, Gustavo
                      and Pan, Jianjun and Matthews, Garrett and Muschol, Martin
                      and Hoyer, Wolfgang},
      title        = {{P}rotofibril‐{F}ibril {I}nteractions {I}nhibit {A}myloid
                      {F}ibril {A}ssembly by {O}bstructing {S}econdary
                      {N}ucleation},
      journal      = {Angewandte Chemie / International edition},
      volume       = {60},
      number       = {6},
      issn         = {1521-3773},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2020-04792},
      pages        = {3016-3021},
      year         = {2021},
      abstract     = {Amyloid-b peptides (Ab) assemble into both rigidamyloid
                      fibrils and metastable oligomers termed AbO orprotofibrils.
                      In Alzheimers disease, Ab fibrils constitute thecore of
                      senile plaques, but Ab protofibrils may represent themain
                      toxic species. Ab protofibrils accumulate at the exterior
                      ofsenile plaques, yet the protofibril–fibril interplay is
                      not wellunderstood. Applying chemical kinetics and atomic
                      forcemicroscopy to the assembly of Ab and lysozyme,
                      protofibrilsare observed to bind to the lateral surfaces of
                      amyloid fibrils.When utilizing Ab variants with different
                      critical oligomerconcentrations, the interaction inhibits
                      the autocatalytic proliferationof amyloid fibrils by
                      secondary nucleation on thefibril surface. Thus, metastable
                      oligomers antagonize theirreplacement by amyloid fibrils
                      both by competing for monomersand blocking secondary
                      nucleation sites. The protofibril—fibril interaction
                      governs their temporal evolution andpotential to exert
                      specific toxic activities.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524) / BETACONTROL - Control of amyloid formation via
                      beta-hairpin molecular recognition features (726368)},
      pid          = {G:(DE-HGF)POF4-5244 / G:(EU-Grant)726368},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33095508},
      UT           = {WOS:000598234800001},
      doi          = {10.1002/anie.202010098},
      url          = {https://juser.fz-juelich.de/record/888243},
}