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@ARTICLE{Hoffmann:9747,
      author       = {Hoffmann, S. and Funke, S. A. and Wiesehan, K. and Moedder,
                      S. and Glück, J.M. and Feuerstein, S.E. and Gerdts, J. and
                      Moetter, J. and Willbold, D.},
      title        = {{C}ompetitively selected protein ligands pay their increase
                      in specificity by a decrease in affinity},
      journal      = {Molecular BioSystems},
      volume       = {6},
      issn         = {1742-206X},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry},
      reportid     = {PreJuSER-9747},
      pages        = {126 - 133},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Protein-ligand interactions characterise and govern the
                      current state and fate of a living cell. The specificity of
                      proteins is mainly determined by the relative affinities to
                      each potential ligand. To investigate the consequences and
                      potentials of ligands with increased specificity in
                      comparison with ligands optimised solely for affinity, it
                      was necessary to identify ligands that are optimised towards
                      specificity instead of a barely optimised affinity to a
                      given target. In the presented example, a modified phage
                      display screening procedure yielded specific ligands for the
                      LckSH3 domain. We found that increased specificity of one of
                      the hereby obtained ligands for LckSH3 is achieved at the
                      cost of a slightly reduced affinity to LckSH3 and a
                      drastically reduced affinity to other SH3 domains. A surface
                      plasmon resonance experiment simulating in vivo-like
                      realistic competitive binding conditions exerted enhanced
                      binding behaviour of the specific ligand under these binding
                      conditions. The experimental data, together with a
                      mathematical model describing the complex experimental
                      situation, and theoretical considerations lead to the
                      conclusion that increased specificity is achieved at the
                      cost of reduced affinity, but after all, it pays if the
                      ligand is applied under realistic, i.e. competitive,
                      conditions.},
      keywords     = {Binding Sites: genetics / Binding Sites: physiology /
                      Ligands / Peptide Library / Protein Binding / Proteins:
                      chemistry / Proteins: metabolism / Surface Plasmon Resonance
                      / src Homology Domains: genetics / src Homology Domains:
                      physiology / Ligands (NLM Chemicals) / Peptide Library (NLM
                      Chemicals) / Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20024074},
      UT           = {WOS:000272875200015},
      doi          = {10.1039/b910945e},
      url          = {https://juser.fz-juelich.de/record/9747},
}