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@ARTICLE{Sieme:916054,
      author       = {Sieme, Daniel and Griesinger, Christian and Rezaie Ghaleh,
                      Nasrollah},
      title        = {{M}etal {B}inding to {S}odium {H}eparin {M}onitored by
                      {Q}uadrupolar {NMR}},
      journal      = {International journal of molecular sciences},
      volume       = {23},
      number       = {21},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2022-05900},
      pages        = {13185 -},
      year         = {2022},
      abstract     = {Heparins and heparan sulfate polysaccharides are negatively
                      charged glycosaminoglycans and play important roles in
                      cell-to-matrix and cell-to-cell signaling processes. Metal
                      ion binding to heparins alters the conformation of heparins
                      and influences their function. Various experimental
                      techniques have been used to investigate metal ion-heparin
                      interactions, frequently with inconsistent results.
                      Exploiting the quadrupolar 23Na nucleus, we herein develop a
                      23Na NMR-based competition assay and monitor the binding of
                      divalent Ca2+ and Mg2+ and trivalent Al3+ metal ions to
                      sodium heparin and the consequent release of sodium ions
                      from heparin. The 23Na spin relaxation rates and
                      translational diffusion coefficients are utilized to
                      quantify the metal ion-induced release of sodium ions from
                      heparin. In the case of the Al3+ ion, the complementary
                      approach of 27Al quadrupolar NMR is employed as a direct
                      probe of ion binding to heparin. Our NMR results demonstrate
                      at least two metal ion-binding sites with different
                      affinities on heparin, potentially undergoing dynamic
                      exchange. For the site with lower metal ion binding
                      affinity, the order of Ca2+ > Mg2+ > Al3+ is obtained, in
                      which even the weakly binding Al3+ ion is capable of
                      displacing sodium ions from heparin. Overall, the
                      multinuclear quadrupolar NMR approach employed here can
                      monitor and quantify metal ion binding to heparin and
                      capture different modes of metal ion-heparin binding.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524) / 5241 - Molecular Information Processing in
                      Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36361973},
      UT           = {WOS:000881191100001},
      doi          = {10.3390/ijms232113185},
      url          = {https://juser.fz-juelich.de/record/916054},
}