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@ARTICLE{Kang:1017753,
      author       = {Kang, Kyongok},
      title        = {{T}he effect of fatty acids, ionic strength, and electric
                      fields on the microscopic dynamics of {BSA} aggregates},
      journal      = {Frontiers in physics},
      volume       = {11},
      issn         = {2296-424X},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {FZJ-2023-04289},
      pages        = {1282099},
      year         = {2023},
      abstract     = {This paper presents the microscopic dynamics of the
                      concentrated suspensions ofbovine serum albumin (BSA)
                      proteins and their aggregates by dynamic lightscattering
                      (DLS) experiments. The effects of fatty acids binding to
                      BSA, as wellas the ionic strength and weak electric field,
                      are discussed for affecting the stabilityof BSA suspensions
                      against calcium-induced aggregation. By variation of the
                      ionicstrength, in the absence of an external electric field,
                      DLS experiments show thatmonomer–BSA interactions (in the
                      essentially fatty acid-free case) are overallrepulsive but
                      that, nevertheless, aggregation occurs to some extent. Also,
                      thediffusive properties of different types of BSA are
                      explored under an applied low-ACelectric field by means of
                      in situ electric small-angle depolarized DLS
                      experiments,which reveal a significant decrease of the
                      translational BSA–monomer diffusioncoefficient with
                      increasing frequency, while the aggregates indicate
                      orientationalmotion via rotation on applying an electric
                      field. These observations areinterpreted in terms of
                      (localized) orientation interactions obtained asoscillations
                      in the intermediate scattering correlation function, as well
                      as theanomalous slower relaxations as resulting in effective
                      (collective) dynamicsbetween monomeric BSA and their protein
                      aggregates.},
      cin          = {IBI-4},
      ddc          = {530},
      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},
      UT           = {WOS:001092372200001},
      doi          = {10.3389/fphy.2023.1282099},
      url          = {https://juser.fz-juelich.de/record/1017753},
}