% 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{Eberle:916401,
      author       = {Eberle, Raphael J. and Sevenich, Marc and Gering, Ian and
                      Scharbert, Lara and Strodel, Birgit and Lakomek, Nils A. and
                      Santur, Karoline and Mohrlüder, Jeannine and Coronado,
                      Mônika A. and Willbold, Dieter},
      title        = {{D}iscovery of {A}ll- d -{P}eptide {I}nhibitors of
                      {SARS}-{C}o{V}-2 3{C}-like {P}rotease},
      journal      = {ACS chemical biology},
      volume       = {18},
      number       = {2},
      issn         = {1554-8929},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2022-06201},
      pages        = {315 - 330},
      year         = {2023},
      abstract     = {During the replication process of SARS-CoV-2, the main
                      protease of the virus [3-chymotrypsin-like protease
                      (3CLpro)] plays a pivotal role and is essential for the life
                      cycle of the pathogen. Numerous studies have been conducted
                      so far, which have confirmed 3CLpro as an attractive drug
                      target to combat COVID-19. We describe a novel and efficient
                      next-generation sequencing (NGS) supported phage display
                      selection strategy for the identification of a set of
                      SARS-CoV-2 3CLpro targeting peptide ligands that inhibit the
                      3CL protease, in a competitive or noncompetitive mode, in
                      the low μM range. From the most efficient l-peptides
                      obtained from the phage display, we designed all-d-peptides
                      based on the retro-inverso (ri) principle. They had IC50
                      values also in the low μM range and in combination, even in
                      the sub-micromolar range. Additionally, the combination with
                      Rutinprivir decreases 10-fold the IC50 value of the
                      competitive inhibitor. The inhibition modes of these d-ri
                      peptides were the same as their respective l-peptide
                      versions. Our results demonstrate that retro-inverso
                      obtained all-d-peptides interact with high affinity and
                      inhibit the SARS-CoV-2 3CL protease, thus reinforcing their
                      potential for further development toward therapeutic agents.
                      The here described d-ri peptides address limitations
                      associated with current l-peptide inhibitors and are
                      promising lead compounds. Further optimization regarding
                      pharmacokinetic properties will allow the development of
                      even more potent d-peptides to be used for the prevention
                      and treatment of COVID-19.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / DFG project 267205415 - SFB 1208: Identität
                      und Dynamik von Membransystemen - von Molekülen bis zu
                      zellulären Funktionen (267205415)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)267205415},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36647580},
      UT           = {WOS:000921927600001},
      doi          = {10.1021/acschembio.2c00735},
      url          = {https://juser.fz-juelich.de/record/916401},
}