% 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{HernndezGonzlez:909091,
      author       = {Hernández González, Jorge E. and Eberle, Raphael J. and
                      Willbold, Dieter and Coronado, Mônika A.},
      title        = {{A} {C}omputer-{A}ided {A}pproach for the {D}iscovery of
                      {D}-{P}eptides as {I}nhibitors of {SARS}-{C}o{V}-2 {M}ain
                      {P}rotease},
      journal      = {Frontiers in molecular biosciences},
      volume       = {8},
      issn         = {2296-889X},
      address      = {Lausanne},
      publisher    = {Frontiers},
      reportid     = {FZJ-2022-03004},
      pages        = {816166},
      year         = {2022},
      abstract     = {The SARS-CoV-2 main protease, also known as
                      3-chymotrypsin-like protease (3CLpro), is a cysteine
                      protease responsible for the cleavage of viral polyproteins
                      pp1a and pp1ab, at least, at eleven conserved sites, which
                      leads to the formation of mature nonstructural proteins
                      essential for the replication of the virus. Due to its
                      essential role, numerous studies have been conducted so far,
                      which have confirmed 3CLpro as an attractive drug target to
                      combat Covid-19 and have reported a vast number of
                      inhibitors and their co-crystal structures. Despite all the
                      ongoing efforts, D-peptides, which possess key advantages
                      over L-peptides as therapeutic agents, have not been
                      explored as potential drug candidates against 3CLpro. The
                      current work fills this gap by reporting an in silico
                      approach for the discovery of D-peptides capable of
                      inhibiting 3CLpro that involves structure-based virtual
                      screening (SBVS) of an in-house library of D-tripeptides and
                      D-tetrapeptides into the protease active site and subsequent
                      rescoring steps, including Molecular Mechanics
                      Generalized-Born Surface Area (MM-GBSA) free energy
                      calculations and molecular dynamics (MD) simulations. In
                      vitro enzymatic assays conducted for the four top-scoring
                      D-tetrapeptides at 20 μM showed that all of them caused
                      $55-85\%$ inhibition of 3CLpro activity, thus highlighting
                      the suitability of the devised approach. Overall, our
                      results present a promising computational strategy to
                      identify D-peptides capable of inhibiting 3CLpro, with
                      broader application in problems involving protein
                      inhibition.},
      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       = {35187076},
      UT           = {WOS:000759912700001},
      doi          = {10.3389/fmolb.2021.816166},
      url          = {https://juser.fz-juelich.de/record/909091},
}