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@ARTICLE{Coronado:858397,
      author       = {Coronado, Monika Aparecida and Eberle, Raphael Josef and
                      Bleffert, Nicole and Feuerstein, Sophie and Olivier, Danilo
                      Silva and de Moraes, Fabio Rogerio and Willbold, Dieter and
                      Arni, Raghuvir Krishnaswamy},
      title        = {{Z}ika virus {NS}2{B}/{NS}3 proteinase: {A} new target for
                      an old drug - {S}uramin a lead compound for {NS}2{B}/{NS}3
                      proteinase inhibition-},
      journal      = {Antiviral research},
      volume       = {160},
      issn         = {0166-3542},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2018-07283},
      pages        = {118 - 125},
      year         = {2018},
      abstract     = {Zika virus infection is the focus of much research due to
                      the medical and social repercussions. Due the role of the
                      viral NS2B/NS3 proteinase in maturation of the viral
                      proteins, it had become an attractive antiviral target.
                      Numerous investigations on viral epidemiology, structure and
                      function analysis, vaccines, and therapeutic drugs have been
                      conducted around the world. At present, no approved vaccine
                      or even drugs have been reported. Thus, there is an urgent
                      need to develop therapeutic agents to cure this epidemic
                      disease. In the present study, we identified the polyanion
                      suramin, an approved antiparasitic drug with antiviral
                      properties, as a potential inhibitor of Zika virus complex
                      NS2B/NS3 proteinase with IC50 of 47 μM. Using
                      fluorescence spectroscopy results we could determine a kd
                      value of 28 μM and had shown that the ligand does not
                      affect the thermal stability of the protein. STD NMR
                      spectroscopy experiments and molecular docking followed by
                      molecular dynamics simulation identified the binding
                      epitopes of the molecule and shows the mode of interaction,
                      respectively. The computational analysis showed that suramin
                      block the Ser135 residue and interact with the catalytically
                      histidine residue.},
      cin          = {ICS-6},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30393012},
      UT           = {WOS:000451936000014},
      doi          = {10.1016/j.antiviral.2018.10.019},
      url          = {https://juser.fz-juelich.de/record/858397},
}