% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Orr:827040,
      author       = {Orr, Asuka A. and Wördehoff and Hoyer, Wolfgang and
                      Tamamis, Phanourios},
      title        = {{U}ncovering the {B}inding and {S}pecificity of
                      β-{W}rapins for {A}myloid-β and α-{S}ynuclein},
      journal      = {The journal of physical chemistry / B},
      volume       = {120},
      number       = {50},
      issn         = {1089-5647},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2017-01246},
      pages        = {12781-12794},
      year         = {2016},
      abstract     = {Amyloidogenic proteins amyloid-β peptide (Aβ) and
                      α-synuclein (α-syn) self-assemble into fibrillar amyloid
                      deposits, senile plaques and Lewy bodies, pathological
                      features of Alzheimer’s and Parkinson’s diseases,
                      respectively. Interestingly, a portion of Alzheimer’s
                      disease cases also exhibit aggregation of α-syn into Lewy
                      bodies, and growing evidence also suggests that Aβ and
                      α-syn oligomers are toxic. Therefore, the simultaneous
                      inhibition through sequestration of the two amyloidogenic
                      proteins may constitute a promising therapeutic strategy.
                      Recently discovered β-wrapin proteins pave the way toward
                      this direction as they can inhibit the aggregation and
                      toxicity of both Aβ and α-syn. Here, we used computational
                      methods, primarily molecular dynamics simulations and free
                      energy calculations, to shed light into the key
                      interaction-based commonalities leading to the dual binding
                      properties of β-wrapins for both amyloidogenic proteins, to
                      identify which interactions potentially act as switches
                      diminishing β-wrapins’ binding activity for Aβ/α-syn,
                      and to examine the binding properties of the current most
                      potent β-wrapin for Aβ. Our analysis provides insights
                      into the distinct role of the key determinants leading to
                      β-wrapin binding to Aβ and α-syn, and suggests that the
                      Aβ 18VFFAED23 and α-syn 38LYVGSK43 are key domains
                      determining the binding specificity of a β-wrapin. Our
                      findings can potentially lead to the discovery of novel
                      therapeutics for Alzheimer’s and Parkinson’s diseases.},
      cin          = {ICS-6},
      ddc          = {530},
      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:000390735800001},
      pubmed       = {pmid:27934063},
      doi          = {10.1021/acs.jpcb.6b08485},
      url          = {https://juser.fz-juelich.de/record/827040},
}