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...
Saved in:
Main Authors: | , |
---|---|
Format: | text |
Published: |
Animo Repository
2019
|
Subjects: | |
Online Access: | https://animorepository.dlsu.edu.ph/faculty_research/6103 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | De La Salle University |
id |
oai:animorepository.dlsu.edu.ph:faculty_research-6908 |
---|---|
record_format |
eprints |
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 |
_version_ |
1767196456215642112 |