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@ARTICLE{Liao:830415,
      author       = {Liao, Qinghua and Owen, Michael and Olubiyi, Olujide and
                      Barz, Bogdan and Strodel, Birgit},
      title        = {{C}onformational {T}ransitions of the {A}myloid-β
                      {P}eptide {U}pon {C}opper({II}) {B}inding and p{H}
                      {C}hanges},
      journal      = {Israel journal of chemistry},
      volume       = {57},
      number       = {7-8},
      issn         = {0021-2148},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2017-03964},
      pages        = {771–784},
      year         = {2017},
      abstract     = {Amyloid-β (Aβ) is a natively unfolded peptide found in
                      all Alzheimer's disease patients as the major component of
                      fibrillar plaques, which are recognized as an important
                      pathological hallmark in Alzheimer's disease. The binding of
                      copper to Aβ increases its neurotoxicity, as Cu2+ causes
                      Aβ to become redox active and decreases the lag time
                      associated with Aβ aggregation. In addition, the pH is a
                      major factor that influences both the Aβ aggregation rates
                      and Cu2+ binding. Hamiltonian replica exchange molecular
                      dynamics (H-REMD) simulations enable atomistic insights into
                      the effects of pH and Cu2+ complexation on the structure and
                      dynamics of Aβ. To study the Aβ1–42/Cu2+ complex, we
                      have developed new force-field parameters for the divalent
                      copper ion ligated by the two histidine residues, His6 and
                      His13, as well as the amine and carbonyl groups of Asp1, in
                      a distorted square-planar geometry. Our comparative
                      simulations reveal that both Cu2+ binding and a low
                      pH-mimicking acidosis, linked to inflammatory processes
                      in vivo, accelerate the formation of β-strands in
                      Aβ1–42 and lead to the stabilization of salt bridges,
                      previously shown to promote Aβ aggregation. The results
                      suggest that Cu2+ binding and mild acidic conditions can
                      shift the conformational equilibrium towards
                      aggregation-prone conformers for the monomeric Aβ.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000407253500019},
      doi          = {10.1002/ijch.201600108},
      url          = {https://juser.fz-juelich.de/record/830415},
}