The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid Bilayer
The interaction of the transmembrane domain of SARS-CoV-2 E-protein with glycyrrhizic acid in a model lipid bilayer (small isotropic bicelles) is demonstrated using various NMR techniques. Glycyrrhizic acid (GA) is the main active component of licorice root, and it shows antiviral activity against v...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-05-01
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| Series: | Membranes |
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| Online Access: | https://www.mdpi.com/2077-0375/13/5/505 |
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| author | Polina A. Kononova Olga Yu. Selyutina Nikolay E. Polyakov |
| author_facet | Polina A. Kononova Olga Yu. Selyutina Nikolay E. Polyakov |
| author_sort | Polina A. Kononova |
| collection | DOAJ |
| description | The interaction of the transmembrane domain of SARS-CoV-2 E-protein with glycyrrhizic acid in a model lipid bilayer (small isotropic bicelles) is demonstrated using various NMR techniques. Glycyrrhizic acid (GA) is the main active component of licorice root, and it shows antiviral activity against various enveloped viruses, including coronavirus. It is suggested that GA can influence the stage of fusion between the viral particle and the host cell by incorporating into the membrane. Using NMR spectroscopy, it was shown that the GA molecule penetrates into the lipid bilayer in a protonated state, but localizes on the bilayer surface in a deprotonated state. The transmembrane domain of SARS-CoV-2 E-protein facilitates deeper GA penetration into the hydrophobic region of bicelles at both acidic and neutral pH and promotes the self-association of GA at neutral pH. Phenylalanine residues of the E-protein interact with GA molecules inside the lipid bilayer at neutral pH. Furthermore, GA influences the mobility of the transmembrane domain of SARS-CoV-2 E-protein in the bilayer. These data provide deeper insight into the molecular mechanism of antiviral activity of glycyrrhizic acid. |
| first_indexed | 2024-03-11T03:30:40Z |
| format | Article |
| id | doaj.art-baf1b03063f34d2ea17b3b7382c3b33b |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-11T03:30:40Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-baf1b03063f34d2ea17b3b7382c3b33b2023-11-18T02:24:24ZengMDPI AGMembranes2077-03752023-05-0113550510.3390/membranes13050505The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid BilayerPolina A. Kononova0Olga Yu. Selyutina1Nikolay E. Polyakov2Voevodsky Institute of Chemical Kinetics and Combustion, Institutskaya str. 3, 630090 Novosibirsk, RussiaVoevodsky Institute of Chemical Kinetics and Combustion, Institutskaya str. 3, 630090 Novosibirsk, RussiaVoevodsky Institute of Chemical Kinetics and Combustion, Institutskaya str. 3, 630090 Novosibirsk, RussiaThe interaction of the transmembrane domain of SARS-CoV-2 E-protein with glycyrrhizic acid in a model lipid bilayer (small isotropic bicelles) is demonstrated using various NMR techniques. Glycyrrhizic acid (GA) is the main active component of licorice root, and it shows antiviral activity against various enveloped viruses, including coronavirus. It is suggested that GA can influence the stage of fusion between the viral particle and the host cell by incorporating into the membrane. Using NMR spectroscopy, it was shown that the GA molecule penetrates into the lipid bilayer in a protonated state, but localizes on the bilayer surface in a deprotonated state. The transmembrane domain of SARS-CoV-2 E-protein facilitates deeper GA penetration into the hydrophobic region of bicelles at both acidic and neutral pH and promotes the self-association of GA at neutral pH. Phenylalanine residues of the E-protein interact with GA molecules inside the lipid bilayer at neutral pH. Furthermore, GA influences the mobility of the transmembrane domain of SARS-CoV-2 E-protein in the bilayer. These data provide deeper insight into the molecular mechanism of antiviral activity of glycyrrhizic acid.https://www.mdpi.com/2077-0375/13/5/505glycyrrhizic acidantiviral activitySARS-CoV-2coronavirus E-proteinlipid membranesNMR |
| spellingShingle | Polina A. Kononova Olga Yu. Selyutina Nikolay E. Polyakov The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid Bilayer Membranes glycyrrhizic acid antiviral activity SARS-CoV-2 coronavirus E-protein lipid membranes NMR |
| title | The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid Bilayer |
| title_full | The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid Bilayer |
| title_fullStr | The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid Bilayer |
| title_full_unstemmed | The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid Bilayer |
| title_short | The Interaction of the Transmembrane Domain of SARS-CoV-2 E-Protein with Glycyrrhizic Acid in Lipid Bilayer |
| title_sort | interaction of the transmembrane domain of sars cov 2 e protein with glycyrrhizic acid in lipid bilayer |
| topic | glycyrrhizic acid antiviral activity SARS-CoV-2 coronavirus E-protein lipid membranes NMR |
| url | https://www.mdpi.com/2077-0375/13/5/505 |
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