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@ARTICLE{Bocharov:905388,
      author       = {Bocharov, Eduard V. and Gremer, Lothar and Urban, Anatoly
                      S. and Okhrimenko, Ivan S. and Volynsky, Pavel E. and
                      Nadezhdin, Kirill D. and Bocharova, Olga V. and Kornilov,
                      Daniil A. and Zagryadskaya, Yuliya A. and Kamynina, Anna V.
                      and Kuzmichev, Pavel K. and Kutzsche, Janine and Bolakhrif,
                      Najoua and Müller-Schiffmann, Andreas and Dencher, Norbert
                      A. and Arseniev, Alexander S. and Efremov, Roman G. and
                      Gordeliy, Valentin I. and Willbold, Dieter},
      title        = {{A}ll - d - {E}nantiomeric {P}eptide {D}3 {D}esigned for
                      {A}lzheimer’s {D}isease {T}reatment {D}ynamically
                      {I}nteracts with {M}embrane-{B}ound {A}myloid-β
                      {P}recursors},
      journal      = {Journal of medicinal chemistry},
      volume       = {64},
      number       = {22},
      issn         = {0022-2623},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2022-00640},
      pages        = {16464 - 16479},
      year         = {2021},
      note         = {Kein Post-print vorhanden},
      abstract     = {Alzheimer’s disease (AD) is a severe neurodegenerative
                      pathology with no effective treatment known. Toxic
                      amyloid-β peptide (Aβ) oligomers play a crucial role in AD
                      pathogenesis. All-d-Enantiomeric peptide D3 and its
                      derivatives were developed to disassemble and destroy
                      cytotoxic Aβ aggregates. One of the D3-like compounds is
                      approaching phase II clinical trials; however,
                      high-resolution details of its disease-preventing or
                      pharmacological actions are not completely clear. We
                      demonstrate that peptide D3 stabilizing Aβ monomer
                      dynamically interacts with the extracellular juxtamembrane
                      region of a membrane-bound fragment of an amyloid precursor
                      protein containing the Aβ sequence. MD simulations based on
                      NMR measurement results suggest that D3 targets the
                      amyloidogenic region, not compromising its α-helicity and
                      preventing intermolecular hydrogen bonding, thus creating
                      prerequisites for inhibition of early steps of Aβ
                      conversion into β-conformation and its toxic
                      oligomerization. An enhanced understanding of the D3 action
                      molecular mechanism facilitates development of effective AD
                      treatment and prevention strategies.},
      cin          = {IBI-7},
      ddc          = {610},
      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       = {pmid:34739758},
      UT           = {WOS:000754726000008},
      doi          = {10.1021/acs.jmedchem.1c00632},
      url          = {https://juser.fz-juelich.de/record/905388},
}