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@ARTICLE{Szal:614105,
      author       = {Szal, Tania and Chauhan, Shweta Singh and Lewe, Philipp and
                      Rachad, Fatima-Zahra and Madre, Marina and Paunina, Laura
                      and Witt, Susanne and Parthasarathi, Ramakrishnan and
                      Windshuegel, Bjoern},
      title        = {{E}fflux {P}ump-{B}inding
                      4(3-{A}minocyclobutyl){P}yrimidin-2-{A}mines {A}re
                      {C}olloidal {A}ggregators},
      journal      = {Biomolecules},
      volume       = {13},
      number       = {6},
      issn         = {2218-273X},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {PUBDB-2024-05739},
      pages        = {1000},
      year         = {2023},
      abstract     = {Efflux pumps are a relevant factor in antimicrobial
                      resistance. In E. coli, the tripartite efflux pump
                      AcrAB-TolC removes a chemically diverse set of antibiotics
                      from the bacterium. Therefore, small molecules interfering
                      with efflux pump function are considered adjuvants for
                      improving antimicrobial therapies. Several compounds
                      targeting the periplasmic adapter protein AcrA and the
                      efflux pump AcrB have been identified to act synergistically
                      with different antibiotics. Among those, several
                      4(3-aminocyclobutyl)pyrimidin-2-amines have been shown to
                      bind to both proteins. In this study, we intended to
                      identify analogs of these substances with improved binding
                      affinity to AcrA using virtual screening followed by
                      experimental validation. While we succeeded in identifying
                      several compounds showing a synergistic effect with
                      erythromycin on E. coli, biophysical studies suggested that
                      4(3-aminocyclobutyl)pyrimidin-2-amines form colloidal
                      aggregates that do not bind specifically to AcrA. Therefore,
                      these substances are not suited for further development. Our
                      study emphasizes the importance of implementing additional
                      control experiments to identify aggregators among bioactive
                      compounds.},
      cin          = {CSSB-CF-PP},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-CF-PP-20210530},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37371580},
      UT           = {WOS:001017057600001},
      doi          = {10.3390/biom13061000},
      url          = {https://bib-pubdb1.desy.de/record/614105},
}