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@ARTICLE{Orr:858403,
      author       = {Orr, Asuka A. and Shaykhalishahi, Hamed and Mirecka, Ewa A.
                      and Jonnalagadda, Sai Vamshi R. and Hoyer, Wolfgang and
                      Tamamis, Phanourios},
      title        = {{E}lucidating the multi-targeted anti-amyloid activity and
                      enhanced islet amyloid polypeptide binding of β-wrapins},
      journal      = {Computers $\&$ chemical engineering},
      volume       = {116},
      issn         = {0098-1354},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2018-07289},
      pages        = {322 - 332},
      year         = {2018},
      abstract     = {β-wrapins are engineered binding proteins stabilizing the
                      β-hairpin conformations of amyloidogenic proteins islet
                      amyloid polypeptide (IAPP), amyloid-β, and α-synuclein,
                      thus inhibiting their amyloid propensity. Here, we use
                      computational and experimental methods to investigate the
                      molecular recognition of IAPP by β-wrapins. We show that
                      the multi-targeted, IAPP, amyloid-β, and α-synuclein,
                      binding properties of β-wrapins originate mainly from
                      optimized interactions between β-wrapin residues and sets
                      of residues in the three amyloidogenic proteins with similar
                      physicochemical properties. Our results suggest that IAPP is
                      a comparatively promiscuous β-wrapin target, probably due
                      to the low number of charged residues in the IAPP β-hairpin
                      motif. The sub-micromolar affinity of β-wrapin HI18,
                      specifically selected against IAPP, is achieved in part by
                      salt-bridge formation between HI18 residue Glu10 and the
                      IAPP N-terminal residue Lys1, both located in the flexible
                      N-termini of the interacting proteins. Our findings provide
                      insights towards developing novel protein-based single- or
                      multi-targeted therapeutics.},
      cin          = {ICS-6},
      ddc          = {660},
      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},
      pubmed       = {pmid:30405276},
      UT           = {WOS:000448410000023},
      doi          = {10.1016/j.compchemeng.2018.02.013},
      url          = {https://juser.fz-juelich.de/record/858403},
}