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@INPROCEEDINGS{Pant:874410,
      author       = {Pant, Pradeep and Ruiz-Blanco, Yasser B. and
                      Sanchez-Garcia, Elsa},
      title        = {{S}olvent {E}ffects on the {B}inding of {F}atty {A}cids to
                      {H}uman {S}erum {A}lbumin},
      volume       = {50},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag},
      reportid     = {FZJ-2020-01420},
      series       = {Publication Series of the John von Neumann Institute for
                      Computing (NIC) NIC Series},
      pages        = {147 - 156},
      year         = {2020},
      comment      = {NIC Symposium 2020},
      booktitle     = {NIC Symposium 2020},
      abstract     = {Solvent interactions can influence the properties and
                      function of complex biomolecules. Among others, altering the
                      solvent composition has consequences for the recognition of
                      binding partners. Human serum albumin (HSA) is one of the
                      most enigmatic biomolecules, known as an efficient carrier
                      of biological materials, such as hormones, fatty acids and
                      drugs. Here we explored the effects of the solvent on
                      stearic acid-HSA binding. To this end, we performed all-atom
                      molecular dynamics (MD) simulations in explicit solvent (~
                      2.9 μs in total). These MD simulations were carried out in
                      explicit water and in a $20\%$ ethanol-water mixture. The
                      sampling in both systems was processed with the MM-PBSA
                      binding free energy approach, which allowed us to
                      investigate the effects of the solvent composition on the
                      binding of stearic acid molecules to seven binding sites of
                      HSA. Using this computational approach, we were able to
                      reproduce the experimental preference of fatty acid’s
                      binding sites for albumin in water. Site 5 > site 4 > site 2
                      were calculated as high affinity fatty acid binding sites,
                      in agreement with the experimental reports.[1]
                      Interestingly, we observed that site 1 becomes the most
                      prominent binding pocket in the $20\%$ ethanol-water
                      mixture, with overall binding affinity towards stearic acid:
                      site 1 > site 5 > site 2. Our simulations in explicit
                      solvent also provided a rationale for this effect.
                      Importantly, we achieved weak binding-to strong binding
                      conversion by using a solvent mixture, with repercussions
                      for the specific binding properties and the manipulation of
                      HSA properties as biological carrier.},
      month         = {Feb},
      date          = {2020-02-27},
      organization  = {NIC Symposium 2020, Jülich (Germany),
                       27 Feb 2020 - 28 Feb 2020},
      cin          = {NIC},
      cid          = {I:(DE-Juel1)NIC-20090406},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)8 / PUB:(DE-HGF)7},
      url          = {https://juser.fz-juelich.de/record/874410},
}