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@ARTICLE{Mirecka:172157,
      author       = {Mirecka, Ewa Agnieszka and Gremer, Lothar and Schiefer,
                      Stephanie and Oesterhelt, Filipp and Stoldt, Matthias and
                      Willbold, Dieter and Hoyer, Wolfgang},
      title        = {{E}ngineered aggregation inhibitor fusion for production of
                      highly amyloidogenic human islet amyloid polypeptide},
      journal      = {Journal of biotechnology},
      volume       = {-},
      issn         = {0168-1656},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2014-05667},
      pages        = {S0168-1656(14)00287-9},
      year         = {2014},
      abstract     = {Human islet amyloid polypeptide (IAPP) is the major
                      component of pancreatic amyloid deposits in type 2 diabetes.
                      The structural conversion of IAPP from a monomeric state
                      into amyloid assemblies is the subject of intense research.
                      Recombinant production of IAPP is, however, difficult due to
                      its extreme aggregation propensity. Here we describe a novel
                      strategy for expression of IAPP in Escherichia coli, based
                      on an engineered protein tag, which sequesters IAPP monomers
                      and prevents IAPP aggregation. The IAPP-binding protein HI18
                      was selected by phage display from a β-wrapin library.
                      Fusion of HI18 to IAPP enabled the soluble expression of the
                      construct. IAPP was cleaved from the fusion construct and
                      purified to homogeneity with a yield of 3mg of isotopically
                      labeled peptide per liter of culture. In the monomeric
                      state, IAPP was largely disordered as evidenced by far-UV CD
                      and liquid-state NMR spectroscopy but competent to form
                      amyloid fibrils according to atomic force microscopy. These
                      results demonstrate the ability of the engineered
                      β-wrapin HI18 for shielding the hydrophobic sequence of
                      IAPP during expression and purification. Fusion of
                      aggregation-inhibiting β-wrapins is a suitable approach
                      for the recombinant production of aggregation-prone
                      proteins.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000345684000028},
      pubmed       = {pmid:24928165},
      doi          = {10.1016/j.jbiotec.2014.06.006},
      url          = {https://juser.fz-juelich.de/record/172157},
}