Probing the vibrational spectroscopic properties and binding mechanism of anti-influenza agent Liquiritin using experime
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Probing the vibrational spectroscopic properties and binding mechanism of anti‑influenza agent Liquiritin using experimental and computational studies B. Sathya1 · S. Karthi2 · K. Ajaijawahar1 · M. Prasath1 Received: 12 April 2020 / Accepted: 13 July 2020 © Springer Nature B.V. 2020
Abstract Liquiritin is an anti-viral agent of H1N1 and H3N2 influenza A virus which was reported to inhibit H1N1 and H3N2 NA enzyme with IC50 value of 82.3 and > 100 μM, respectively. The ground state optimized geometry was carried out for Liquiritin molecule through DFT method. The experimental vibrational (FT-IR and FT-Raman) and electronic (UV–Vis) spectral information were analysed and compared with theoretical data. The MEP and Fukui functions were determined for Liquiritin to analyse the electrophilic and nucleophilic attack of the molecule. The NBO and HOMO–LUMO were concluded for Liquiritin to investigate the chemical reactivity and kinetic stability. The druglikeness and ADMET predictions were analysed for Liquiritin, and it confirms the Lipinski’s rule of five. Liquiritin fits very well in the active site cavity of H1N1 and H3N2 NA enzyme with binding energies of − 6.36 and − 5.87 kcal mol−1 and inhibition constants (21.76 and 49.98 ki UM micromol), respectively, through docking study. Consequently, the molecule reveals good biological behaviour in nature and it can act as a probable drug candidate for H1N1 and H3N2 viral influenza. Keywords DFT · UV–Vis · FT-IR · FT-Raman · Influenza · Neuraminidase
Introduction Influenza (flu) A virus is a worldwide annual pandemic and epidemic respiratory infectious diseases which is caused by RNA virus belongs to the Orthomyxoviridae family [1], and it causes huge mortality and morbidity in humans [2]. The flu * M. Prasath [email protected] 1
Department of Physics, Periyar University PG Extension Centre, Dharmapuri, Tamilnadu 636701, India
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Henan Key Laboratory of Polyoxometalate Chemistry, College of Chemistry and Chemical Engineering, Henan University, Kaifeng 47504, People’s Republic of China
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spread among animals and human beings through contact with bronchial epithelial cells [3]. Influenza A is branched into subcategories based on Hemagglutinin (HA) (18 subcategories) and Neuraminidase (NA) (11 subcategories) in this subtypes H1N1 and H3N2 are endemic in humans [4, 5]. Influenza has two glycoproteins specifically HA [6] and NA [7]. HA was a cell-anchoring viral glycoprotein which is responsible for viral infection via linking monosaccharide sialic acid having receptors on the host cells and mediating the entry and fusion of virus [8]. NA (sialidase) is a hydrolytic viral glycoprotein which is feasible for cleaving of sialic acid from surface of the cell and also to release the progeny virus particles from host cells [9]. The influenza viruses implement numerous prospective molecular targets for drug discovery. Amid these targets, NA is one of the promising ways to treat influenza virus because of NA can secure the host
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