The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I

The anti-venom activity of Andrographis paniculata (Burm.f.) Nees roots (APR) dichloromethane crude extracts and a promising APR constituent, skullcapflavone I (SKI) was investigated by monitoring the inhibition of secretory phospholipase A 2 (sPLA 2) of Naja philippinensis Taylor venom (NPV) crysta...

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Main Authors: Tan, Maria Carmen S., Tan, Daisylyn Senna Y.
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Published: Animo Repository 2019
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Online Access:https://animorepository.dlsu.edu.ph/faculty_research/6103
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Institution: De La Salle University
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spelling oai:animorepository.dlsu.edu.ph:faculty_research-69082022-07-27T03:04:38Z The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I Tan, Maria Carmen S. Tan, Daisylyn Senna Y. The anti-venom activity of Andrographis paniculata (Burm.f.) Nees roots (APR) dichloromethane crude extracts and a promising APR constituent, skullcapflavone I (SKI) was investigated by monitoring the inhibition of secretory phospholipase A 2 (sPLA 2) of Naja philippinensis Taylor venom (NPV) crystallized samples. Gas chromatography-mass spectrometry was used for the characterization of extracts, while molecular docking was utilized to understand anti-venom properties. Chromatographic analyses primarily revealed the presence of methoxylated flavones. NPV was found to have sPLA 2 activity (0.0796 ± 0.0018 μmol/minutes/ml) that has been attributed to the poisonous effects. SKI (IC 50 : 51.1 ± 3.5 μg/ml), isolated from APR showed strong inhibitory effect on phospholipase activity compared with dichloromethane extracts of APR (IC 50 : 192.7 ± 10.9 μg/ml) indicating that SKI was the cause of the bioactivity in APR. Molecular docking simulations showed corresponding results with highly negative binding energies (−6.59 to −8.72 kcal/mol) predicted for the binding of SKI to PLA 2 proteins. An important trend found was the presence of free bound Ca 2+ lowered binding energies signifying that Ca 2+ a has role in the binding of the SKI to PLA 2 proteins. The anti-venom property of APR and the pure compound SKI, upon further studies, could be the first line of defense in the medical protocol of snake venom neutralization. 2019-03-01T08:00:00Z text https://animorepository.dlsu.edu.ph/faculty_research/6103 Faculty Research Work Animo Repository Acanthaceae—Analysis Antivenins Biochemistry, Biophysics, and Structural Biology
institution De La Salle University
building De La Salle University Library
continent Asia
country Philippines
Philippines
content_provider De La Salle University Library
collection DLSU Institutional Repository
topic Acanthaceae—Analysis
Antivenins
Biochemistry, Biophysics, and Structural Biology
spellingShingle Acanthaceae—Analysis
Antivenins
Biochemistry, Biophysics, and Structural Biology
Tan, Maria Carmen S.
Tan, Daisylyn Senna Y.
The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I
description The anti-venom activity of Andrographis paniculata (Burm.f.) Nees roots (APR) dichloromethane crude extracts and a promising APR constituent, skullcapflavone I (SKI) was investigated by monitoring the inhibition of secretory phospholipase A 2 (sPLA 2) of Naja philippinensis Taylor venom (NPV) crystallized samples. Gas chromatography-mass spectrometry was used for the characterization of extracts, while molecular docking was utilized to understand anti-venom properties. Chromatographic analyses primarily revealed the presence of methoxylated flavones. NPV was found to have sPLA 2 activity (0.0796 ± 0.0018 μmol/minutes/ml) that has been attributed to the poisonous effects. SKI (IC 50 : 51.1 ± 3.5 μg/ml), isolated from APR showed strong inhibitory effect on phospholipase activity compared with dichloromethane extracts of APR (IC 50 : 192.7 ± 10.9 μg/ml) indicating that SKI was the cause of the bioactivity in APR. Molecular docking simulations showed corresponding results with highly negative binding energies (−6.59 to −8.72 kcal/mol) predicted for the binding of SKI to PLA 2 proteins. An important trend found was the presence of free bound Ca 2+ lowered binding energies signifying that Ca 2+ a has role in the binding of the SKI to PLA 2 proteins. The anti-venom property of APR and the pure compound SKI, upon further studies, could be the first line of defense in the medical protocol of snake venom neutralization.
format text
author Tan, Maria Carmen S.
Tan, Daisylyn Senna Y.
author_facet Tan, Maria Carmen S.
Tan, Daisylyn Senna Y.
author_sort Tan, Maria Carmen S.
title The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I
title_short The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I
title_full The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I
title_fullStr The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I
title_full_unstemmed The anti-venom potential of Andrographis paniculata (Burm.f.) Nees roots and its constituent skullcapflavone I
title_sort anti-venom potential of andrographis paniculata (burm.f.) nees roots and its constituent skullcapflavone i
publisher Animo Repository
publishDate 2019
url https://animorepository.dlsu.edu.ph/faculty_research/6103
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