Docking and molecular dynamics studies of human ezrin protein with a modelled SARS-CoV-2 endodomain and their interaction with potential invasion inhibitors
Chellasamy et al.,
Docking and molecular dynamics studies of human ezrin protein with a modelled SARS-CoV-2 endodomain and their..,
Journal of King Saud University - Science, doi:10.1016/j.jksus.2022.102277
In Silico study of SARS-CoV-1&2 endodomains and ezrin docking, identifying ivermectin, quercetin, calcifediol, calcitriol, selamectin, and minocycline as potential therapeutic drugs with strong ezrin binding which may restrict viral endodomain interaction while also stabilizing ezrin, thereby reducing virus fusion and infection.
Chellasamy et al., 10 Aug 2022, peer-reviewed, 2 authors.
Contact:
selvaakumar.c@dypatil.edu, eleanorwatson@connect.glos.ac.uk.
In Silico studies are an important part of preclinical research, however results may be very different in vivo.
Abstract: Journal Pre-proofs
Original article
Docking and molecular dynamics studies of human ezrin protein with a mod‐
elled SARS-CoV-2 endodomain and their interaction with potential invasion
inhibitors
Selvaa Kumar Chellasamy, Eleanor Watson
PII:
DOI:
Reference:
S1018-3647(22)00458-X
https://doi.org/10.1016/j.jksus.2022.102277
JKSUS 102277
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Journal of King Saud University - Science
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Revised Date:
Accepted Date:
16 June 2021
1 August 2022
8 August 2022
Please cite this article as: S.K. Chellasamy, E. Watson, Docking and molecular dynamics studies of human ezrin
protein with a modelled SARS-CoV-2 endodomain and their interaction with potential invasion inhibitors,
Journal of King Saud University - Science (2022), doi: https://doi.org/10.1016/j.jksus.2022.102277
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Docking and molecular dynamics studies of human ezrin
protein with a modelled SARS-CoV-2 endodomain and their
interaction with potential invasion inhibitors
Selvaa Kumar Chellasamy 1*, and Eleanor Watson 2,*
School of Biotechnology and Bioinformatics, D. Y. Patil Deemed to be University, Sector-15, CBD Belapur,
Navi Mumbai, 400614, India; e-mail: selvaakumar.c@dypatil.edu
2 School of Computing & Engineering, University of Gloucestershire; e-mail:
eleanorwatson@connect.glos.ac.uk
* Correspondence: e-mails: selvaakumar.c@dypatil.edu (SKC); Tel.: +91-022-68797900 (SKC) and
eleanorwatson@connect.glos.ac.uk (EW) available at Nell Watson Ltd, c/o Mills Pyatt, 11 Kingfisher
Business Park, Arthur Street, Redditch, Worcestershire, B98 8LG, United Kingdom
1
Declaration of Interests: None.
Docking and molecular dynamics studies of human ezrin
protein with a modelled SARS-CoV-2 endodomain and their
interaction with potential invasion inhibitors
Abstract: Human ezrin protein interacts with SARS-CoV S endodomain and restrict the virus fusion,
entry, and their early events of infection. In general, their binding strength and their structural
stability determines their entry into the host cells. However, the binding affinity of these two
endodomains with the ezrin protein has been elusive due to a paucity of knowledge on the 3D
structure. This study modelled the endodomains of both SARS-CoV-1 and SARS-CoV-2 and then
docked these models with human ezrin protein. This study establishes that the modelled
endodomains of both SARS-CoV-1 and SARS-Cov-2 consisted of three disulphide bridges for selfstabilization. Protein-protein docking listed four salt bridges with a higher buried surface area
between ezrin-SARS-CoV-1 endodomain compared to that of ezrin-SARS-CoV-2 with six salt
bridges with lower buried surface area. Molecular simulation of the ezrin-SARS-CoV-1 endodomain
showed better structural stability with lower Root Mean Square Deviation score compared to that
of ezrin-SARS-CoV-2 endodomain due to the substitution of Alanine with..
chellasamy
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