% 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{Lai:909710,
      author       = {Lai, Hien T. T. and Nguyen, Ly H. and Phan, Anh D. and
                      Kranjc Pietrucci, Agata and Nguyen, Toan T. and Nguyen-Manh,
                      Duc},
      title        = {{A} comparative study of receptor interactions between
                      {SARS}-{C}o{V} and {SARS}-{C}o{V}-2 from molecular modeling},
      journal      = {Journal of molecular modeling},
      volume       = {28},
      number       = {10},
      issn         = {0948-5023},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {FZJ-2022-03358},
      pages        = {305},
      year         = {2022},
      abstract     = {The pandemic of COVID-19 severe acute respiratory syndrome,
                      which was fatal for millions of people worldwide,
                      triggeredthe race to understand in detail the molecular
                      mechanisms of this disease. In this work, the differences of
                      interactions betweenthe SARS-CoV/SARS-CoV-2 Receptor binding
                      domain (RBD) and the human Angiotensin Converting Enzyme 2
                      (ACE2)receptor were studied using in silico tools. Our
                      results show that SARS-CoV-2 RBD is more stable and forms
                      more interactionswith ACE2 than SARS-CoV. At its interface,
                      three stable binding patterns are observed and named
                      red-K31, green-K353 and blue-M82 according to the central
                      ACE2 binding residue. In SARS-CoV instead, only the first
                      two binding patchesare persistently formed during the MD
                      simulation. Our MM/GBSA calculations indicate the binding
                      free energy differenceof about 2.5 kcal/mol between
                      SARS-CoV-2 and SARS-CoV which is compatible with the
                      experiments. The binding freeenergy decomposition points out
                      that SARS-CoV-2 RBD–ACE2 interactions of the red-K31 (
                      −23.5 ± 0.2 kcal∕mol ) andblue-M82 ( −9.1 ± 0.1
                      kcal∕mol ) patterns contribute more to the binding
                      affinity than in SARS-CoV ( −1.8 ± 0.02 kcal∕molfor
                      red-K31), while the contribution of the green-K353 pattern
                      is very similar in the two strains ( −17.8 ± 0.2
                      kcal∕moland −22.7 ± 0.1 kcal∕mol for SARS-CoV-2 and
                      SARS-CoV, respectively). Five groups of mutations draw our
                      attentionat the RBD–ACE2 binding interface, among them,
                      the mutation –PPA469-471/GVEG482-485 has the most
                      important andfavorable impact on SARS-CoV-2 binding to the
                      ACE2 receptor. These results, highlighting the molecular
                      differences in thebinding between the two viruses,
                      contribute to the common knowledge about the new corona
                      virus and to the developmentof appropriate antiviral
                      treatments, addressing the necessity of ongoing pandemics.},
      cin          = {INM-9 / IAS-5},
      ddc          = {540},
      cid          = {I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36074206},
      UT           = {WOS:000852403700002},
      doi          = {10.1007/s00894-022-05231-7},
      url          = {https://juser.fz-juelich.de/record/909710},
}