Poster Talk: The use of Computational Docking to estimate the effects of Montelukast on potential viral main protease catalytic site

A Case for Montelukast in COVID-19: “The use of Computational Docking to estimate the effects of Montelukast on potential viral main protease catalytic site “

Salman Mansoor1, Shoab Saadat2, Aitzaz Amin3, Imran Ali4, Muhammad Tauseef Ghaffar5, Usman Amin6, Muhammad Fahad7 ,Mohsin Mukhtar8

1 Registrar Neurology, Department of Neurology, Sligo University Hospital, Sligo, Ireland

2 Renal trainee and Data Scientist, Department of Nephrology, Mid-essex Hospitals, NHS Trust, United Kingdom

3, 5 Registrar Medicine, Department of Medicine, Sligo University Hospital, Sligo, Ireland

4 Rheumatology Trainee, Department of Rheumatology, Sligo University Hospital, Sligo, Ireland

6 Rheumatology Trainee, Department of Rheumatology, Waterford University Hospital, Waterford, Ireland

7 Registrar Nephrology, Department of Nephrology, Sligo University Hospital, Sligo, Ireland

8 Registrar Medicine, Department of Endocrinology, St.Luke’s Regional Hospital, Kilkenny, Ireland

Corresponding Author: Dr Salman Mansoor, Registrar Neurology, Sligo University Hospital, Sligo, Ireland

This article explores the possible role of Montelukast in management of SARS-CoV-2 infection after reviewing the available literature and further uses computational docking to estimate the effects of Montelukast on the main protease inhibitor site of SARS-CoV-2.

Methodology: In this study, we used molecular docking to estimate the direct effects of Montelukast on the main protease (Mpro) inhibitor site of the SARS-CoV-2. While other studies have been performed on the homology models, we obtained the Mpro crystalized structure, A-chain (304 amino acid residues) from protein data bank (PDB code 5REK) for this analysis

Results: The best docked Montelukast conformer had a mfscore of -71.68 and was seen to be making multiple hydrogen bonds with the neighbouring residues (T24, T24, T26, S46) with the closest bond with T24 (Distance= 1.71 angstrom). Important finding was its hydrogen bond with H41 and hydrophobic interactions with C145 as these residues for important members of the active catalytics site.