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@ARTICLE{Eberle:908872,
      author       = {Eberle, Raphael J. and Gering, Ian and Tusche, Markus and
                      Ostermann, Philipp N. and Müller, Lisa and Adams, Ortwin
                      and Schaal, Heiner and Olivier, Danilo S. and Amaral, Marcos
                      S. and Arni, Raghuvir K. and Willbold, Dieter and Coronado,
                      Mônika A.},
      title        = {{D}esign of {D}-{A}mino {A}cids {SARS}-{C}o{V}-2 {M}ain
                      {P}rotease {I}nhibitors {U}sing the {C}ationic {P}eptide
                      from {R}attlesnake {V}enom as a {S}caffold},
      journal      = {Pharmaceuticals},
      volume       = {15},
      number       = {5},
      issn         = {1424-8247},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2022-02886},
      pages        = {540 -},
      year         = {2022},
      abstract     = {The C30 endopeptidase (3C-like protease; 3CLpro) is
                      essential for the life cycle of SARS-CoV-2 (severe acute
                      respiratory syndrome-coronavirus-2) since it plays a pivotal
                      role in viral replication and transcription and, hence, is a
                      promising drug target. Molecules isolated from animals,
                      insects, plants, or microorganisms can serve as a scaffold
                      for the design of novel biopharmaceutical products.
                      Crotamine, a small cationic peptide from the venom of the
                      rattlesnake Crotalus durissus terrificus, has been the focus
                      of many studies since it exhibits activities such as
                      analgesic, in vitro antibacterial, and hemolytic activities.
                      The crotamine derivative L-peptides (L-CDP) that inhibit the
                      3CL protease in the low µM range were examined since they
                      are susceptible to proteolytic degradation; we explored the
                      utility of their D-enantiomers form. Comparative uptake
                      inhibition analysis showed D-CDP as a promising prototype
                      for a D-peptide-based drug. We also found that the
                      D-peptides can impair SARS-CoV-2 replication in vivo,
                      probably targeting the viral protease 3CLpro.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35631367},
      UT           = {WOS:000803447200001},
      doi          = {10.3390/ph15050540},
      url          = {https://juser.fz-juelich.de/record/908872},
}