The application of in silico experimental model in the assessment of ciprofloxacin and levofloxacin interaction with main SARS-CoV-2 targets : S-, E- and TMPRSS2 proteins, RNA-dependent RNA polymerase and papain-like protease (PLpro)-preliminary molecular docking analysis

© 2021. The Author(s)..

BACKGROUND: The new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified at the end of 2019. Despite growing understanding of SARS-CoV-2 in virology as well as many molecular studies, except remdesivir, no specific anti-SARS-CoV-2 drug has been officially approved.

METHODS: In the present study molecular docking technique was applied to test binding affinity of ciprofloxacin and levofloxacin-two commercially available fluoroquinolones, to SARS-CoV-2 S-, E- and TMPRSS2 proteins, RNA-dependent RNA polymerase and papain-like protease (PLPRO). Chloroquine and dexamethasone were used as reference positive controls.

RESULTS: When analyzing the molecular docking data it was noticed that ciprofloxacin and levofloxacin possess lower binding energy with S protein as compared to the references. In the case of TMPRSS2 protein and PLPRO protease the best docked ligand was levofloxacin and in the case of E proteins and RNA-dependent RNA polymerase the best docked ligands were levofloxacin and dexamethasone. Moreover, a molecular dynamics study also reveals that ciprofloxacin and levofloxacin form a stable complex with E- and TMPRSS2 proteins, RNA polymerase and papain-like protease (PLPRO).

CONCLUSIONS: The revealed data indicate that ciprofloxacin and levofloxacin could interact and potentially inhibit crucial SARS-CoV-2 proteins.

Media Type:

Electronic Article

Year of Publication:

2021

Contained In:

Pharmacological reports : PR - Vol. 73, No. 6 (2021), p. 1765-1780

Language:

English

Contributors:

Marciniec, Krzysztof
Beberok, Artur
Boryczka, Stanisław
Wrześniok, Dorota

Links:

Volltext

Keywords:

E protein
Fluoroquinolones
Journal Article
Papain-like protease (PLPRO)
RNA-dependent RNA polymerase
S protein
TMPRSS2 protein

Notes:

Date Revised 18.11.2021

published: Print-Electronic

Citation Status In-Process

Copyright: From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Physical Description:

Online-Ressource

doi:

10.1007/s43440-021-00282-8

PMID:

34052981

PPN (Catalogue-ID):

NLM327168900