% 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{Maity:888244,
      author       = {Maity, Debabrata and Kumar, Sunil and AlHussein, Ruyof and
                      Gremer, Lothar and Howarth, Madeline and Karpauskaite, Laura
                      and Hoyer, Wolfgang and Magzoub, Mazin and Hamilton, Andrew
                      D.},
      title        = {{S}ub-stoichiometric inhibition of {IAPP} aggregation: a
                      peptidomimetic approach to anti-amyloid agents},
      journal      = {RSC chemical biology},
      volume       = {1},
      number       = {4},
      issn         = {2633-0679},
      address      = {Cambridge},
      publisher    = {The Royal Society of Chemistry},
      reportid     = {FZJ-2020-04793},
      pages        = {225-232},
      year         = {2020},
      abstract     = {Membrane-catalysed misfolding of islet amyloid polypeptide
                      is associated with the death of β-cells in type II diabetes
                      (T2D). Most active compounds so far reported require high
                      doses for inhibition of membrane bound IAPP fibrillation.
                      Here, we describe a naphthalimide-appended
                      oligopyridylamide-based α-helical mimetic, DM 1, for
                      targeting membrane bound IAPP. DM 1 completely inhibits the
                      aggregation of IAPP at doses of 0.2 equivalents. DM 1 is
                      also effective at similarly low doses for inhibition of
                      seed-catalyzed secondary nucleation. An NMR based study
                      demonstrates that DM 1 modulates IAPP self-assembly by
                      stabilizing and/or perturbing the N-terminus helix
                      conformation. DM 1 at substoichiometric doses rescues rat
                      insulinoma cells from IAPP-mediated cytotoxicity. Most
                      importantly, 0.2 equivalents of DM 1 disaggregate preformed
                      oligomers and fibrils and can reverse cytotoxicity by
                      modulating toxic preformed oligomers and fibrils of IAPP
                      into non-toxic conformations.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000616568300007},
      doi          = {10.1039/D0CB00086H},
      url          = {https://juser.fz-juelich.de/record/888244},
}