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@ARTICLE{Niether:838073,
      author       = {Niether, Doreen and Kawaguchi, Tsubasa and Hovancová, Jana
                      and Eguchi, Kazuya and Dhont, Jan K. G. and Kita, Rio and
                      Wiegand, Simone},
      title        = {{R}ole of {H}ydrogen {B}onding of {C}yclodextrin–{D}rug
                      {C}omplexes {P}robed by {T}hermodiffusion},
      journal      = {Langmuir},
      volume       = {33},
      number       = {34},
      issn         = {1520-5827},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2017-06811},
      pages        = {8483 - 8492},
      year         = {2017},
      abstract     = {The temperature-gradient induced migration of biomolecules,
                      known as thermophoresis or thermodiffusion, changes upon
                      ligand binding. In recent years, this effect has been used
                      to determine protein-ligand binding constants. The mechanism
                      through which thermodiffusive properties change when
                      complexes are formed, however, is not understood. An
                      important contribution to thermodiffusive properties
                      originates from the thermal response of hydrogen bonds.
                      Since there is a considerable difference between the degree
                      of solvation of the protein-ligand complex and its isolated
                      components, ligand-binding is accompanied by a significant
                      change in hydration. The aim of the present work is
                      therefore to investigate the role played by hydrogen bonding
                      on the change in thermodiffusive behaviour upon ligand
                      binding. As a model system we use cyclodextrins (CDs) and
                      acetylsalicylic acid (ASA), where a quite significant change
                      in hydration is expected, and where no conformational
                      changes occur when a CD-ASA complex is formed in aqueous
                      solution. Thermophoresis was investigated in a temperature
                      range from 10 to 50°C by infrared thermal diffusion forced
                      Rayleigh scattering (IR-TDFRS). NMR measurements were
                      performed at 25°C to obtain information about the structure
                      of the complexes. All CD-ASA complexes show a stronger
                      affinity towards regions of lower temperature as compared to
                      the free CDs. We found that the temperature sensitivity of
                      thermophoresis correlates with the 1-octanol/water partition
                      coefficient. This observation not only establishes the
                      relation between thermodiffusion and the degree of hydrogen
                      bonding, but also opens the possibility to relate
                      thermodiffusive properties of complexes to their partition
                      coefficient, which can not be determined otherwise. This
                      concept is especially interesting for protein-ligand
                      complexes where the protein undergoes a conformational
                      change, different from the CD-ASA complexes, giving rise to
                      additional changes in their hydrophilicity.},
      cin          = {ICS-3},
      ddc          = {670},
      cid          = {I:(DE-Juel1)ICS-3-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000409292500016},
      doi          = {10.1021/acs.langmuir.7b02313},
      url          = {https://juser.fz-juelich.de/record/838073},
}