% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Bouckaert:168260,
      author       = {Bouckaert, Julie and Li, Zhaoli and Xavier, Catarina and
                      Almant, Mehdi and Caveliers, Vicky and Lahoutte, Tony and
                      Weeks, Stephen and Kovensky, José and Gouin, Sébastien G.},
      title        = {{H}eptyl α- {D} -{M}annosides {G}rafted on a
                      β-{C}yclodextrin {C}ore {T}o {I}nterfere with {E}scherichia
                      coli {A}dhesion: {A}n {I}n {V}ivo {M}ultivalent {E}ffect},
      journal      = {Chemistry},
      volume       = {19},
      number       = {24},
      issn         = {0947-6539},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {DESY-2014-02452},
      pages        = {7847 - 7855},
      year         = {2013},
      note         = {© WILEY‐VCH Verlag GmbH $\&$ Co. KGaA, Weinheim},
      abstract     = {n‐Heptyl α‐D‐mannoside (HM) has previously been
                      identified as a nanomolar FimH antagonist able to prevent
                      Escherichia coli adhesion. We have designed mono‐ and
                      heptavalent glycoconjugates in which HM is tethered to
                      β‐cyclodextrin (β‐CD) through short and long spacers.
                      One‐pot click or co‐clicking procedures were developed
                      to directly obtain the glycoconjugates from unprotected HM
                      and β‐CD precursors. These FimH antagonists were examined
                      biophysically and in vivo. Reverse titrations by isothermal
                      calorimetry led to trapping of the short‐tethered
                      heptavalent β‐CD in a complex with three FimH lectins.
                      Combined dynamic light scattering and small‐angle X‐ray
                      solution scattering data allowed the construction of a model
                      of the FimH trimer. The heptavalent β‐CDs were shown to
                      capture and aggregate living bacteria in solution and are
                      therefore also able to aggregate FimH when attached to
                      different bacteria pili. The first in vivo evaluation of
                      multivalent FimH inhibitors has been performed. The
                      heptavalent β‐CDs proved to be much more effective
                      anti‐adhesive agents than monovalent references with doses
                      of around 2 μg instilled in the mouse bladder leading to
                      a significantly decreased E. coli load. Intravenously
                      injected radiolabeled glycoconjugates can rapidly reach the
                      mouse bladder and >2 μg concentrations can easily be
                      retained over 24 h to prevent fluxing bacteria from
                      rebinding.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {FS Beamline without reference (POF2-544)},
      pid          = {G:(DE-H253)POF2-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000319825500025},
      pubmed       = {pmid:23595913},
      doi          = {10.1002/chem.201204015},
      url          = {https://bib-pubdb1.desy.de/record/168260},
}