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@ARTICLE{Mastalipour:1046365,
      author       = {Mastalipour, Mohammadamin and Gering, Ian and Coronado,
                      Mônika Aparecida and González, Jorge Enrique Hernández
                      and Willbold, Dieter and Eberle, Raphael Josef},
      title        = {{N}ovel peptide inhibitor for the {C}hikungunya virus
                      ns{P}2 protease: {I}dentification and characterization},
      journal      = {Current research in microbial sciences},
      volume       = {8},
      issn         = {2666-5174},
      address      = {Amsterdam},
      publisher    = {Elsevier B.V.},
      reportid     = {FZJ-2025-03793},
      pages        = {100376 -},
      year         = {2025},
      abstract     = {Chikungunya virus (CHIKV) is an emerging pathogen affecting
                      populations worldwide, with rapidly increasing infection
                      rates. CHIKV, an arbovirus of the alphavirus genus, is
                      predominantly found in tropical regions and transmitted by
                      Aedes mosquitoes. Climate change has accelerated the global
                      spread of these vectors, leading to outbreaks in
                      non-tropical regions, including parts of Europe. The absence
                      of antiviral therapies and the potential for co-infections
                      with other viruses make CHIKV a significant public health
                      concern. CHIKV replication relies on nsP2 cysteine protease
                      activity to cleave its viral polyprotein into functional
                      nonstructural and structural proteins. Targeting the nsP2
                      protease represents a promising strategy for antiviral
                      therapy development. In this study, phage display was used
                      to screen a library of peptides for potential binders of the
                      target protease. Biophysical and biochemical analyses of the
                      identified peptides assessed their inhibitory potential.
                      Among the six identified peptides (named as P1–P6), four
                      demonstrated inhibitory effects on the nsP2 protease
                      (nsP2pro). Peptide P1 exhibited the strongest inhibitory
                      effect, with a half-maximal inhibitory concentration (IC50)
                      of 4.6 ± 1.9 µM, and a low cytotoxicity. The secondary
                      structure analysis through CD spectroscopy and homology
                      modelling revealed that P1 adopts an alpha-helical
                      conformation. Finally, molecular dynamics simulations
                      enabled us to investigate the dynamics of the nsP2pro active
                      site and molecular docking was employed to predict the
                      orthosteric binding mode of P1, providing insights into
                      protein-peptide interaction. These findings underscore the
                      potential of peptide P1 as a lead compound for further
                      investigation in the context of CHIKV research.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {40165933},
      UT           = {WOS:001448662000001},
      doi          = {10.1016/j.crmicr.2025.100376},
      url          = {https://juser.fz-juelich.de/record/1046365},
}