% 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{Mirecka:821077,
      author       = {Mirecka, Ewa A. and Feuerstein, Sophie and Gremer, Lothar
                      and Schröder, Gunnar F. and Stoldt, Matthias and Willbold,
                      Dieter and Hoyer, Wolfgang},
      title        = {β-{H}airpin of {I}slet {A}myloid {P}olypeptide {B}ound to
                      an {A}ggregation {I}nhibitor},
      journal      = {Scientific reports},
      volume       = {6},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2016-06321},
      pages        = {33474 -},
      year         = {2016},
      abstract     = {In type 2 diabetes, the formation of islet amyloid
                      consisting of islet amyloid polypeptide (IAPP) isassociated
                      with reduction in β-cell mass and contributes to the
                      failure of islet cell transplantation.Rational design of
                      inhibitors of IAPP amyloid formation has therapeutic
                      potential, but is hampered bythe lack of structural
                      information on inhibitor complexes of the conformationally
                      flexible, aggregationproneIAPP. Here we characterize a
                      β-hairpin conformation of IAPP in complex with the
                      engineeredbinding protein β-wrapin HI18. The β-strands
                      correspond to two amyloidogenic motifs, 12-LANFLVH-18and
                      22-NFGAILS-28, which are connected by a turn established
                      around Ser-20. Besides backbonehydrogen bonding, the
                      IAPP:HI18 interaction surface is dominated by non-polar
                      contacts involvinghydrophobic side chains of the IAPP
                      β-strands. Apart from monomers, HI18 binds oligomers and
                      fibrilsand inhibits IAPP aggregation and toxicity at low
                      substoichiometric concentrations. The IAPP β-hairpincan
                      serve as a molecular recognition motif enabling control of
                      IAPP aggregation.},
      cin          = {ICS-6},
      ddc          = {000},
      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:000383383100001},
      pubmed       = {pmid:27641459},
      doi          = {10.1038/srep33474},
      url          = {https://juser.fz-juelich.de/record/821077},
}