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@ARTICLE{Nachbar:130216,
      author       = {M. Nachbar and S. El Deeb and M. Mozafari and H. A. Alhazmi
                      and L. Preu and S. Redweik and W. D. Lehmann$^*$ and H.
                      Wätzig},
      title        = {{C}a(2+) -complex stability of {GAPAGPLIVPY} peptide in gas
                      and aqueous phase, investigated by affinity capillary
                      electrophoresis and molecular dynamics simulations and
                      compared to mass spectrometric results.},
      journal      = {Electrophoresis},
      volume       = {37},
      number       = {5-6},
      issn         = {0173-0835},
      address      = {Weinheim},
      publisher    = {Wiley-Blackwell},
      reportid     = {DKFZ-2017-05296},
      pages        = {744 - 751},
      year         = {2016},
      abstract     = {Strong, sequence-specific gas-phase bindings between
                      proline-rich peptides and alkaline earth metal ions in
                      nanoESI-MS experiments were reported by Lehmann et al.
                      (Rapid Commun. Mass Spectrom. 2006, 20, 2404-2410), however
                      its relevance for physiological-like aqueous phase is
                      uncertain. Therefore, the complexes should also be studied
                      in aqueous solution and the relevance of the MS method for
                      binding studies be evaluated. A mobility shift ACE method
                      was used for determining the binding between the small
                      peptide GAPAGPLIVPY and various metal ions in aqueous
                      solution. The findings were compared to the MS results and
                      further explained using computational methods. While the MS
                      data showed a strong alkaline earth ion binding, the ACE
                      results showed nonsignificant binding. The proposed vacuum
                      state complex also decomposed during a molecular dynamic
                      simulation in aqueous solution. This study shows that the
                      formed stable peptide-metal ion adducts in the gas phase by
                      ESI-MS does not imply the existence of analogous adducts in
                      the aqueous phase. Comparing peptide-metal ion interaction
                      under the gaseous MS and aqueous ACE conditions showed huge
                      difference in binding behavior.},
      keywords     = {Gases (NLM Chemicals) / Peptides (NLM Chemicals) / Calcium
                      (NLM Chemicals)},
      cin          = {W160},
      ddc          = {570},
      cid          = {I:(DE-He78)W160-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26627117},
      doi          = {10.1002/elps.201500403},
      url          = {https://inrepo02.dkfz.de/record/130216},
}