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@ARTICLE{Kang:911209,
      author       = {Kang, Kyongok and Platten, Florian},
      title        = {{E}lectric-{F}ield {I}nduced {M}odulation of {A}morphous
                      {P}rotein {A}ggregates: {P}olarization, {D}eformation, and
                      {R}eorientation},
      journal      = {Scientific reports},
      volume       = {12},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2022-04514},
      pages        = {3061},
      year         = {2022},
      abstract     = {Proteins in their native state are only marginally stable
                      and tend to aggregate. However, proteinmisfolding and
                      condensation are often associated with undesired processes,
                      such as pathogenesis, orunwanted properties, such as reduced
                      biological activity, immunogenicity, or uncontrolled
                      materialsproperties. Therefore, controlling protein
                      aggregation is very important, but still a major challengein
                      various fields, including medicine, pharmacology, food
                      processing, and materials science. Here,flexible, amorphous,
                      micron-sized protein aggregates composed of lysozyme
                      molecules reduced bydithiothreitol are used as a model
                      system. The preformed amorphous protein aggregates are
                      exposedto a weak alternating current electric field. Their
                      field response is followed in situ by time-resolvedpolarized
                      optical microscopy, revealing field-induced deformation,
                      reorientation and enhancedpolarization as well as the
                      disintegration of large clusters of aggregates. Small-angle
                      dynamiclight scattering was applied to probe the collective
                      microscopic dynamics of amorphous aggregatesuspensions.
                      Field-enhanced local oscillations of the intensity
                      auto-correlation function are observedand related to two
                      distinguishable elastic moduli. Our results validate the
                      prospects of electric fieldsfor controlling protein
                      aggregation processes.},
      cin          = {IBI-4},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IBI-4-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35197521},
      UT           = {WOS:000760421800038},
      doi          = {10.1038/s41598-022-06995-x},
      url          = {https://juser.fz-juelich.de/record/911209},
}