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Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein
Angiotensin converting enzyme 2 (ACE2) and main protease (M(Pro)) are significant target proteins, mainly involved in the attachment of viral genome to host cells and aid in replication of severe acute respiratory syndrome‐coronaviruses or SARS‐CoV genome. In the present study, we identified 11 pote...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7361879/ https://www.ncbi.nlm.nih.gov/pubmed/32838301 http://dx.doi.org/10.1002/fft2.29 |
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author | Poochi, Saravana Prabha Easwaran, Murugesh Balasubramanian, Balamuralikrishnan Anbuselvam, Mohan Meyyazhagan, Arun Park, Sungkwon Bhotla, Haripriya Kuchi Anbuselvam, Jeeva Arumugam, Vijaya Anand Keshavarao, Sasikala Kanniyappan, Gopalakrishnan Velliyur Pappusamy, Manikantan Kaul, Tanushri |
author_facet | Poochi, Saravana Prabha Easwaran, Murugesh Balasubramanian, Balamuralikrishnan Anbuselvam, Mohan Meyyazhagan, Arun Park, Sungkwon Bhotla, Haripriya Kuchi Anbuselvam, Jeeva Arumugam, Vijaya Anand Keshavarao, Sasikala Kanniyappan, Gopalakrishnan Velliyur Pappusamy, Manikantan Kaul, Tanushri |
author_sort | Poochi, Saravana Prabha |
collection | PubMed |
description | Angiotensin converting enzyme 2 (ACE2) and main protease (M(Pro)) are significant target proteins, mainly involved in the attachment of viral genome to host cells and aid in replication of severe acute respiratory syndrome‐coronaviruses or SARS‐CoV genome. In the present study, we identified 11 potent bioactive compounds from ethanolic leaf extract of Ipomoea obscura (L.) by using GC‐MS analysis. These potential bioactive compounds were considered for molecular docking studies against ACE2 and M(Pro) target proteins to determine the antiviral effects against SARS‐COV. Results exhibits that among 11 compounds from I. obscura (L.), urso‐deoxycholic acid, demeclocycline, tetracycline, chlorotetracycline, and ethyl iso‐allocholate had potential viral inhibitory activity. Hence, the present findings suggested that chemical constitution present in I. obscura (L.) will address inhibition of corona viral replication in host cells. |
format | Online Article Text |
id | pubmed-7361879 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-73618792020-07-15 Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein Poochi, Saravana Prabha Easwaran, Murugesh Balasubramanian, Balamuralikrishnan Anbuselvam, Mohan Meyyazhagan, Arun Park, Sungkwon Bhotla, Haripriya Kuchi Anbuselvam, Jeeva Arumugam, Vijaya Anand Keshavarao, Sasikala Kanniyappan, Gopalakrishnan Velliyur Pappusamy, Manikantan Kaul, Tanushri Food Front Research Articles Angiotensin converting enzyme 2 (ACE2) and main protease (M(Pro)) are significant target proteins, mainly involved in the attachment of viral genome to host cells and aid in replication of severe acute respiratory syndrome‐coronaviruses or SARS‐CoV genome. In the present study, we identified 11 potent bioactive compounds from ethanolic leaf extract of Ipomoea obscura (L.) by using GC‐MS analysis. These potential bioactive compounds were considered for molecular docking studies against ACE2 and M(Pro) target proteins to determine the antiviral effects against SARS‐COV. Results exhibits that among 11 compounds from I. obscura (L.), urso‐deoxycholic acid, demeclocycline, tetracycline, chlorotetracycline, and ethyl iso‐allocholate had potential viral inhibitory activity. Hence, the present findings suggested that chemical constitution present in I. obscura (L.) will address inhibition of corona viral replication in host cells. John Wiley and Sons Inc. 2020-07-06 2020-06 /pmc/articles/PMC7361879/ /pubmed/32838301 http://dx.doi.org/10.1002/fft2.29 Text en © 2020 The Authors. Food Frontiers published by NCU, NWU, JSU, ZJU & FAFU and John Wiley & Sons Australia, Ltd https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Poochi, Saravana Prabha Easwaran, Murugesh Balasubramanian, Balamuralikrishnan Anbuselvam, Mohan Meyyazhagan, Arun Park, Sungkwon Bhotla, Haripriya Kuchi Anbuselvam, Jeeva Arumugam, Vijaya Anand Keshavarao, Sasikala Kanniyappan, Gopalakrishnan Velliyur Pappusamy, Manikantan Kaul, Tanushri Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein |
title | Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein |
title_full | Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein |
title_fullStr | Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein |
title_full_unstemmed | Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein |
title_short | Employing bioactive compounds derived from Ipomoea obscura (L.) to evaluate potential inhibitor for SARS‐CoV‐2 main protease and ACE2 protein |
title_sort | employing bioactive compounds derived from ipomoea obscura (l.) to evaluate potential inhibitor for sars‐cov‐2 main protease and ace2 protein |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7361879/ https://www.ncbi.nlm.nih.gov/pubmed/32838301 http://dx.doi.org/10.1002/fft2.29 |
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