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@ARTICLE{Pounot:890913,
      author       = {Pounot, Kevin and Grime, Geoffrey W. and Longo, Alessandro
                      and Zamponi, Michaela and Noferini, Daria and Cristiglio,
                      Viviana and Seydel, Tilo and Garman, Elspeth F. and Weik,
                      Martin and Foderà, Vito and Schirò, Giorgio},
      title        = {{Z}inc determines dynamical properties and aggregation
                      kinetics of human insulin},
      journal      = {Biophysical journal},
      volume       = {120},
      number       = {5},
      issn         = {0006-3495},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2021-01244},
      pages        = {886},
      year         = {2021},
      abstract     = {Protein aggregation is a widespread process leading to
                      deleterious consequences in the organism, with amyloid
                      aggregates being important not only in biology but also for
                      drug design and biomaterial production. Insulin is a protein
                      largely used in diabetes treatment, and its amyloid
                      aggregation is at the basis of the so-called insulin-derived
                      amyloidosis. Here, we uncover the major role of zinc in both
                      insulin dynamics and aggregation kinetics at low pH, in
                      which the formation of different amyloid superstructures
                      (fibrils and spherulites) can be thermally induced. Amyloid
                      aggregation is accompanied by zinc release and the
                      suppression of water-sustained insulin dynamics, as shown by
                      particle-induced x-ray emission and x-ray absorption
                      spectroscopy and by neutron spectroscopy, respectively. Our
                      study shows that zinc binding stabilizes the native form of
                      insulin by facilitating hydration of this hydrophobic
                      protein and suggests that introducing new binding sites for
                      zinc can improve insulin stability and tune its aggregation
                      propensity.},
      cin          = {JCNS-FRM-II / JCNS-1 / JCNS-4 / MLZ},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-4-20201012 /
                      I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33545104},
      UT           = {WOS:000630953600016},
      doi          = {10.1016/j.bpj.2020.11.2280},
      url          = {https://juser.fz-juelich.de/record/890913},
}