% 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{CarballoPacheco:279306,
      author       = {Carballo-Pacheco, Martín and Ismail, Ahmed E. and Strodel,
                      Birgit},
      title        = {{O}ligomer {F}ormation of {T}oxic and {F}unctional
                      {A}myloid {P}eptides {S}tudied with {A}tomistic
                      {S}imulations},
      journal      = {The journal of physical chemistry / B},
      volume       = {119},
      number       = {30},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2015-07321},
      pages        = {9696 - 9705},
      year         = {2015},
      abstract     = {Amyloids are associated with diseases, including
                      Alzheimer’s, as well as functional roles such as storage
                      of peptide hormones. It is still unclear what differences
                      exist between aberrant and functional amyloids. However, it
                      is known that soluble oligomers formed during amyloid
                      aggregation are more toxic than the final fibrils. Here, we
                      perform molecular dynamics simulations to study the
                      aggregation of the amyloid-β peptide Aβ25–35, associated
                      with Alzheimer’s disease, and two functional
                      amyloid-forming tachykinin peptides: kassinin and neuromedin
                      K. Although the three peptides have similar primary
                      sequences, tachykinin peptides, in contrast to Aβ25–35,
                      form nontoxic amyloids. Our simulations reveal that the
                      charge of the C-terminus is essential to controlling the
                      aggregation process. In particular, when the kassinin
                      C-terminus is not amidated, the aggregation kinetics
                      decreases considerably. In addition, we observe that the
                      monomeric peptides in extended conformations aggregate
                      faster than those in collapsed hairpin-like conformations.},
      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:000359031400022},
      pubmed       = {pmid:26130191},
      doi          = {10.1021/acs.jpcb.5b04822},
      url          = {https://juser.fz-juelich.de/record/279306},
}