Critical Interactions between the SARS-CoV-2 Spike Glycoprotein and the Human ACE2 Receptor

Elhan Taka, Sema Z. Yilmaz, Mert Golcuk, Ceren Kilinc, Umut Aktas, Ahmet Yildiz, Mert Gur*

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33 Atıf (Scopus)


Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects human cells by binding its spike (S) glycoproteins to angiotensin-converting enzyme 2 (ACE2) receptors and causes the coronavirus disease 2019 (COVID-19). Therapeutic approaches to prevent SARS-CoV-2 infection are mostly focused on blocking S-ACE2 binding, but critical residues that stabilize this interaction are not well understood. By performing all-atom molecular dynamics (MD) simulations, we identified an extended network of salt bridges, hydrophobic and electrostatic interactions, and hydrogen bonds between the receptor-binding domain (RBD) of the S protein and ACE2. Mutagenesis of these residues on the RBD was not sufficient to destabilize binding but reduced the average work to unbind the S protein from ACE2. In particular, the hydrophobic end of RBD serves as the main anchor site and is the last to unbind from ACE2 under force. We propose that blocking the hydrophobic surface of RBD via neutralizing antibodies could prove to be an effective strategy to inhibit S-ACE2 interactions.

Orijinal dilİngilizce
Sayfa (başlangıç-bitiş)5537-5548
Sayfa sayısı12
DergiJournal of Physical Chemistry B
Basın numarası21
Yayın durumuYayınlandı - 3 Haz 2021

Bibliyografik not

Publisher Copyright:
© 2021 American Chemical Society. All rights reserved.


This work used resources services, and support provided via the COVID-19 HPC Consortium (, which is a unique private-public effort to bring together government, industry, and academic leaders who are volunteering free compute time and resources in support of COVID-19 research. E.T., S.Z.Y., M.G. (Mert Golcuk), C.K., and U.A. were supported during this study through the Scientific and Technological Research Council of Turkey (TUBITAK) 2247-C Intern Research Fellowship Program. This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. This work is supported by the COVID-19 HPC Consortium (grant numbers: TG-MCB200070 and TG-BIO200053 ) and TUBITAK (2247-C Intern Research Fellowship Program).

FinansörlerFinansör numarası
HPC ConsortiumTG-MCB200070, TG-BIO200053
National Science FoundationACI-1548562
Türkiye Bilimsel ve Teknolojik Araştirma Kurumu

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