Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular Characterization
Neuraminidase (NA) is an enzyme that prevents virions from aggregating within the host cell and promotes cell-to-cell spread by cleaving glycosidic linkages to sialic acid. The best-known neuraminidase is the viral neuraminidase, which present in the influenza virus. Thus, the development of anti-in...
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MDPI AG
2022-01-01
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| Series: | Molecules |
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| author | Muchtaridi Muchtaridi Rina Fajri Nuwarda Emmy Hainida Khairul Ikram Aisyah Saad Abdul Rahim Amirah Mohd Gazzali Habibah A. Wahab |
| author_facet | Muchtaridi Muchtaridi Rina Fajri Nuwarda Emmy Hainida Khairul Ikram Aisyah Saad Abdul Rahim Amirah Mohd Gazzali Habibah A. Wahab |
| author_sort | Muchtaridi Muchtaridi |
| collection | DOAJ |
| description | Neuraminidase (NA) is an enzyme that prevents virions from aggregating within the host cell and promotes cell-to-cell spread by cleaving glycosidic linkages to sialic acid. The best-known neuraminidase is the viral neuraminidase, which present in the influenza virus. Thus, the development of anti-influenza drugs that inhibit NA has emerged as an important and intriguing approach in the treatment of influenza. <i>Garcinia atroviridis</i> L. (GA) dried fruits (GAF) are used commercially as seasoning and in beverages. The main objective of this study was to identify a new potential neuraminidase inhibitor from GA. A bioassay-guided fractionation method was applied to obtain the bioactive compounds leading to the identification of garcinia acid and naringenin. In an enzyme inhibition study, garcinia acid demonstrated the highest activity when compared to naringenin. Garcinia acid had the highest activity, with an IC<sub>50</sub> of 17.34–17.53 µg/mL or 91.22–92.21 µM against <i>Clostridium perfringens</i>-NA, and 56.71–57.85 µg/mL or 298.32–304.31 µM against H1N1-NA. Based on molecular docking results, garcinia acid interacted with the triad arginine residues (Arg118, Arg292, and Arg371) of the viral neuraminidase, implying that this compound has the potential to act as a NA enzyme inhibitor. |
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| language | English |
| last_indexed | 2024-03-09T23:27:36Z |
| publishDate | 2022-01-01 |
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| record_format | Article |
| series | Molecules |
| spelling | doaj.art-b6a3fd98b5a3425a8491ba9b684e05f12023-11-23T17:15:07ZengMDPI AGMolecules1420-30492022-01-0127394910.3390/molecules27030949Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular CharacterizationMuchtaridi Muchtaridi0Rina Fajri Nuwarda1Emmy Hainida Khairul Ikram2Aisyah Saad Abdul Rahim3Amirah Mohd Gazzali4Habibah A. Wahab5Functional Nano Powder University Center of Excellence (FiNder U CoE), Universitas Padjadajaran, Jl. Bandung-Sumedang KM 21, Jatinangor 45363, IndonesiaDepartment of Pharmaceutical Analysis and Medicinal Chemistry, Faculty of Pharmacy, Universitas Padjadjaran, Jl. Bandung-Sumedang KM 21, Jatinangor 45363, IndonesiaFaculty of Health Sciences, Universiti Teknologi MARA, Bandar Puncak Alam 42300, MalaysiaFaculty of Pharmacy, Universiti Teknologi MARA, Bandar Puncak Alam 42300, MalaysiaSchool of Pharmaceutical Sciences, Universiti Sains Malaysia, Minden 11800, MalaysiaSchool of Pharmaceutical Sciences, Universiti Sains Malaysia, Minden 11800, MalaysiaNeuraminidase (NA) is an enzyme that prevents virions from aggregating within the host cell and promotes cell-to-cell spread by cleaving glycosidic linkages to sialic acid. The best-known neuraminidase is the viral neuraminidase, which present in the influenza virus. Thus, the development of anti-influenza drugs that inhibit NA has emerged as an important and intriguing approach in the treatment of influenza. <i>Garcinia atroviridis</i> L. (GA) dried fruits (GAF) are used commercially as seasoning and in beverages. The main objective of this study was to identify a new potential neuraminidase inhibitor from GA. A bioassay-guided fractionation method was applied to obtain the bioactive compounds leading to the identification of garcinia acid and naringenin. In an enzyme inhibition study, garcinia acid demonstrated the highest activity when compared to naringenin. Garcinia acid had the highest activity, with an IC<sub>50</sub> of 17.34–17.53 µg/mL or 91.22–92.21 µM against <i>Clostridium perfringens</i>-NA, and 56.71–57.85 µg/mL or 298.32–304.31 µM against H1N1-NA. Based on molecular docking results, garcinia acid interacted with the triad arginine residues (Arg118, Arg292, and Arg371) of the viral neuraminidase, implying that this compound has the potential to act as a NA enzyme inhibitor.https://www.mdpi.com/1420-3049/27/3/949neuraminidase<i>Garcinia atroviridis</i>influenza virus |
| spellingShingle | Muchtaridi Muchtaridi Rina Fajri Nuwarda Emmy Hainida Khairul Ikram Aisyah Saad Abdul Rahim Amirah Mohd Gazzali Habibah A. Wahab Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular Characterization Molecules neuraminidase <i>Garcinia atroviridis</i> influenza virus |
| title | Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular Characterization |
| title_full | Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular Characterization |
| title_fullStr | Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular Characterization |
| title_full_unstemmed | Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular Characterization |
| title_short | Neuraminidase Inhibitor of <i>Garcinia atroviridis</i> L. Fruits and Leaves Using Partial Purification and Molecular Characterization |
| title_sort | neuraminidase inhibitor of i garcinia atroviridis i l fruits and leaves using partial purification and molecular characterization |
| topic | neuraminidase <i>Garcinia atroviridis</i> influenza virus |
| url | https://www.mdpi.com/1420-3049/27/3/949 |
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