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@ARTICLE{LeguizamonHerrera:917333,
      author       = {Leguizamon Herrera, Vivian Lorena and Buell, Alexander K.
                      and Willbold, Dieter and Barz, Bogdan},
      title        = {{I}nteraction of {T}herapeutic d -{P}eptides with {A}β42
                      {M}onomers, {T}hermodynamics, and {B}inding {A}nalysis},
      journal      = {ACS chemical neuroscience},
      volume       = {13},
      number       = {11},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2023-00561},
      pages        = {1638 - 1650},
      year         = {2022},
      abstract     = {The aggregation of the amyloid-β (Aβ) peptide is a major
                      hallmark of Alzheimer’s disease. This peptide can
                      aggregate into oligomers, proto-fibrils, and mature fibrils,
                      which eventually assemble into amyloid plaques. The peptide
                      monomers are the smallest assembly units and play an
                      important role in most of the individual processes involved
                      in amyloid fibril formation, such as primary and secondary
                      nucleation and elongation. Several d-peptides have been
                      confirmed as promising candidates to inhibit the aggregation
                      of Aβ into toxic oligomers and fibrils by specifically
                      interacting with monomeric species. In this work, we
                      elucidate the structural interaction and thermodynamics of
                      binding between three d-peptides (D3, ANK6, and RD2) and
                      Aβ42 monomers by means of enhanced molecular dynamics
                      simulations. Our study derives thermodynamic energies in
                      good agreement with experimental values and suggests that
                      there is an enhanced binding for D3 and ANK6, which leads to
                      more stable complexes than for RD2. The binding of D3 to
                      Aβ42 is shown to be weakly exothermic and mainly
                      entropically driven, whereas the complex formation between
                      the ANK6 and RD2 with the Aβ42 free monomer is weakly
                      endothermic. In addition, the changes in the
                      solvent-accessible surface area and the radius of gyration
                      support that the binding between Aβ42 and d-peptides is
                      mainly driven by electrostatic and hydrophobic interactions
                      and leads to more compact conformations.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35580288},
      UT           = {WOS:000819923000001},
      doi          = {10.1021/acschemneuro.2c00102},
      url          = {https://juser.fz-juelich.de/record/917333},
}