INHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>

Envenomation by snakes of the genus Bothrops are a health problem in some tropical countries, not only because of the mortality but given the high percentage of physical disabilities it causes. Phospholipases A2 (PLA2) are abundant constituents in bothropic and crotalic venoms, characterized by indu...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Tatiana LOBO E., Jaime A. PEREAÑEZ, Karol Zapata A., Pablo A. GUTIÉRREZ, Mónica LONDOÑO, Vitelbina NÚÑEZ, Benjamín A. ROJANO
Formato: article
Lenguaje:EN
Publicado: Universidad de Antioquia 2010
Materias:
Acceso en línea:https://doaj.org/article/eab16061d7a04ea783a735ec4c30b271
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:eab16061d7a04ea783a735ec4c30b271
record_format dspace
spelling oai:doaj.org-article:eab16061d7a04ea783a735ec4c30b2712021-11-19T04:14:16ZINHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>0121-40042145-2660https://doaj.org/article/eab16061d7a04ea783a735ec4c30b2712010-11-01T00:00:00Zhttps://revistas.udea.edu.co/index.php/vitae/article/view/7436https://doaj.org/toc/0121-4004https://doaj.org/toc/2145-2660Envenomation by snakes of the genus Bothrops are a health problem in some tropical countries, not only because of the mortality but given the high percentage of physical disabilities it causes. Phospholipases A2 (PLA2) are abundant constituents in bothropic and crotalic venoms, characterized by inducing irreversible muscle damage. Due to the contribution of plants in the snakebite treatment, we focus on the search of phospholipases inhibitors, either as an alternative treatment or as a therapeutic adjuvant of the current treatments. From a screening of 37 vascular plants and bryophytes in the search for such inhibitors, the species Murraya paniculata was selected due to its promising preliminary activity. Starting from this point further work consisting of bioassay-guided fractionation followed by the evaluation of the inhibitory activity of PLA2, the metabolites responsible for the activity were detected through a tandem of gas chromatography - mass spectrometry in the most active fraction, to propose substrate-enzyme inhibition model. The aims of this project was the search of promising compounds with an inhibitory activity of the PLA2 in vascular plants such as M. paniculata, that could become tools for developing new products to improve the prognosis of the snakebite.Tatiana LOBO E.Jaime A. PEREAÑEZKarol Zapata A.Pablo A. GUTIÉRREZMónica LONDOÑOVitelbina NÚÑEZBenjamín A. ROJANOUniversidad de Antioquiaarticlephospholipase A<sub>2</sub><I>Murraya paniculata</I><I>Bothrops</I>molecular docking.Food processing and manufactureTP368-456Pharmaceutical industryHD9665-9675ENVitae, Vol 17, Iss 3 (2010)
institution DOAJ
collection DOAJ
language EN
topic phospholipase A<sub>2</sub>
<I>Murraya paniculata</I>
<I>Bothrops</I>
molecular docking.
Food processing and manufacture
TP368-456
Pharmaceutical industry
HD9665-9675
spellingShingle phospholipase A<sub>2</sub>
<I>Murraya paniculata</I>
<I>Bothrops</I>
molecular docking.
Food processing and manufacture
TP368-456
Pharmaceutical industry
HD9665-9675
Tatiana LOBO E.
Jaime A. PEREAÑEZ
Karol Zapata A.
Pablo A. GUTIÉRREZ
Mónica LONDOÑO
Vitelbina NÚÑEZ
Benjamín A. ROJANO
INHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>
description Envenomation by snakes of the genus Bothrops are a health problem in some tropical countries, not only because of the mortality but given the high percentage of physical disabilities it causes. Phospholipases A2 (PLA2) are abundant constituents in bothropic and crotalic venoms, characterized by inducing irreversible muscle damage. Due to the contribution of plants in the snakebite treatment, we focus on the search of phospholipases inhibitors, either as an alternative treatment or as a therapeutic adjuvant of the current treatments. From a screening of 37 vascular plants and bryophytes in the search for such inhibitors, the species Murraya paniculata was selected due to its promising preliminary activity. Starting from this point further work consisting of bioassay-guided fractionation followed by the evaluation of the inhibitory activity of PLA2, the metabolites responsible for the activity were detected through a tandem of gas chromatography - mass spectrometry in the most active fraction, to propose substrate-enzyme inhibition model. The aims of this project was the search of promising compounds with an inhibitory activity of the PLA2 in vascular plants such as M. paniculata, that could become tools for developing new products to improve the prognosis of the snakebite.
format article
author Tatiana LOBO E.
Jaime A. PEREAÑEZ
Karol Zapata A.
Pablo A. GUTIÉRREZ
Mónica LONDOÑO
Vitelbina NÚÑEZ
Benjamín A. ROJANO
author_facet Tatiana LOBO E.
Jaime A. PEREAÑEZ
Karol Zapata A.
Pablo A. GUTIÉRREZ
Mónica LONDOÑO
Vitelbina NÚÑEZ
Benjamín A. ROJANO
author_sort Tatiana LOBO E.
title INHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>
title_short INHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>
title_full INHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>
title_fullStr INHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>
title_full_unstemmed INHIBITORY ACTIVITY OF <I>Murraya paniculata</I> AGAINST MYOTOXIC PHOSPHOLIPASES A<SUB>2</SUB>
title_sort inhibitory activity of <i>murraya paniculata</i> against myotoxic phospholipases a<sub>2</sub>
publisher Universidad de Antioquia
publishDate 2010
url https://doaj.org/article/eab16061d7a04ea783a735ec4c30b271
work_keys_str_mv AT tatianaloboe inhibitoryactivityofimurrayapaniculataiagainstmyotoxicphospholipasesasub2sub
AT jaimeapereanez inhibitoryactivityofimurrayapaniculataiagainstmyotoxicphospholipasesasub2sub
AT karolzapataa inhibitoryactivityofimurrayapaniculataiagainstmyotoxicphospholipasesasub2sub
AT pabloagutierrez inhibitoryactivityofimurrayapaniculataiagainstmyotoxicphospholipasesasub2sub
AT monicalondono inhibitoryactivityofimurrayapaniculataiagainstmyotoxicphospholipasesasub2sub
AT vitelbinanunez inhibitoryactivityofimurrayapaniculataiagainstmyotoxicphospholipasesasub2sub
AT benjaminarojano inhibitoryactivityofimurrayapaniculataiagainstmyotoxicphospholipasesasub2sub
_version_ 1718420526651670528