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@ARTICLE{Kisonaite:205426,
      author       = {Kisonaite, Migle and Zubrienė, Asta and Čapkauskaitė,
                      Edita and Smirnov, Alexey and Smirnovienė, Joana and
                      Kairys, Visvaldas and Michailovienė, Vilma and Manakova,
                      Elena and Gražulis, Saulius and Matulis, Daumantas},
      title        = {{I}ntrinsic {T}hermodynamics and {S}tructure {C}orrelation
                      of {B}enzenesulfonamides with a {P}yrimidine {M}oiety
                      {B}inding to {C}arbonic {A}nhydrases {I}, {II}, {VII},
                      {XII}, and {XIII}},
      journal      = {PLoS one},
      volume       = {9},
      number       = {12},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2015-00003},
      pages        = {1-26},
      year         = {2014},
      note         = {OA},
      abstract     = {The early stage of drug discovery is often based on
                      selecting the highest affinitylead compound. To this end the
                      structural and energetic characterization of thebinding
                      reaction is important. The binding energetics can be
                      resolved into enthalpicand entropic contributions to the
                      binding Gibbs free energy. Most compoundbinding reactions
                      are coupled to the absorption or release of protons by the
                      proteinor the compound. A distinction between the observed
                      and intrinsic parameters ofthe binding energetics requires
                      the dissection of the protonation/deprotonationprocesses.
                      Since only the intrinsic parameters can be correlated with
                      molecularstructural perturbations associated with complex
                      formation, it is these parametersthat are required for
                      rational drug design. Carbonic anhydrase (CA) isoforms
                      areimportant therapeutic targets to treat a range of
                      disorders including glaucoma,obesity, epilepsy, and cancer.
                      For effective treatment isoform-specific inhibitors
                      areneeded. In this work we investigated the binding and
                      protonation energetics ofsixteen
                      [(2-pyrimidinylthio)acetyl]benzenesulfonamide CA inhibitors
                      usingisothermal titration calorimetry and fluorescent
                      thermal shift assay. The compoundswere built by combining
                      four sulfonamide headgroups with four tailgroups yielding16
                      compounds. Their intrinsic binding thermodynamics showed the
                      limitations ofthe functional group energetic additivity
                      approach used in fragment-based drugdesign, especially at
                      the level of enthalpies and entropies of binding.
                      Combinedwith high resolution crystal structural data
                      correlations were drawn between thechemical functional
                      groups on selected inhibitors and intrinsic
                      thermodynamicparameters of CA-inhibitor complex formation.},
      cin          = {EMBL-User},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {DORIS Beamline K1.1 (POF2-54G13) / MOBILI - Strengthening
                      and Sustaining the European Perspectives of Molecular
                      Biotechnology in Lithuania (245721)},
      pid          = {G:(DE-H253)POF2-K1.1-20130405 / G:(EU-Grant)245721},
      experiment   = {EXP:(DE-H253)D-K1.1-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000346611400031},
      pubmed       = {pmid:25493428},
      doi          = {10.1371/journal.pone.0114106},
      url          = {https://bib-pubdb1.desy.de/record/205426},
}