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Therapeutic application of natural inhibitors against snake venom phospholipase A(2)

Natural inhibitors occupy an important place in the potential to neutralize the toxic effects caused by snake venom proteins and enzymes. It has been well recognized for several years that animal sera, some of the plant and marine extracts are the most potent in neutralizing snake venom phospholipas...

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Autores principales: Perumal Samy, Ramar, Gopalakrishnakone, Ponnampalam, Chow, Vincent TK
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3282276/
https://www.ncbi.nlm.nih.gov/pubmed/22359435
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author Perumal Samy, Ramar
Gopalakrishnakone, Ponnampalam
Chow, Vincent TK
author_facet Perumal Samy, Ramar
Gopalakrishnakone, Ponnampalam
Chow, Vincent TK
author_sort Perumal Samy, Ramar
collection PubMed
description Natural inhibitors occupy an important place in the potential to neutralize the toxic effects caused by snake venom proteins and enzymes. It has been well recognized for several years that animal sera, some of the plant and marine extracts are the most potent in neutralizing snake venom phospholipase A(2) (svPLA(2)). The implication of this review to update the latest research work which has been accomplished with svPLA(2) inhibitors from various natural sources like animal, marine organisms presents a compilation of research in this field over the past decade and revisiting the previous research report including those found in plants. In addition to that the bioactive compounds/inhibitor molecules from diverse sources like aristolochic alkaloid, flavonoids and neoflavonoids from plants, hydrocarbones ­2, 4 dimethyl hexane, 2 methylnonane, and 2, 6 dimethyl heptane obtained from traditional medicinal plants Tragia involucrata (Euphorbiaceae) member of natural products involved for the inhibitory potential of phospholipase A(2) (PLA(2)) enzymes in vitro and also decrease both oedema induced by snake venom as well as human synovial fluid PLA(2). Besides marine natural products that inhibit PLA(2) are manoalide and its derivatives such as scalaradial and related compounds, pseudopterosins and vidalols, tetracylne from synthetic chemicals etc. There is an overview of the role of PLA(2) in inflammation that provides a rationale for seeking inhibitors of PLA(2) as anti-inflammatory agents. However, more studies should be considered to evaluate antivenom efficiency of sera and other agents against a variety of snake venoms found in various parts of the world. The implications of these new groups of svPLA(2) toxin inhibitors in the context of our current understanding of snake biology as well as in the development of new novel antivenoms therapeutics agents in the efficient treatment of snake envenomations are discussed.
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spelling pubmed-32822762012-02-22 Therapeutic application of natural inhibitors against snake venom phospholipase A(2) Perumal Samy, Ramar Gopalakrishnakone, Ponnampalam Chow, Vincent TK Bioinformation Current Trends Natural inhibitors occupy an important place in the potential to neutralize the toxic effects caused by snake venom proteins and enzymes. It has been well recognized for several years that animal sera, some of the plant and marine extracts are the most potent in neutralizing snake venom phospholipase A(2) (svPLA(2)). The implication of this review to update the latest research work which has been accomplished with svPLA(2) inhibitors from various natural sources like animal, marine organisms presents a compilation of research in this field over the past decade and revisiting the previous research report including those found in plants. In addition to that the bioactive compounds/inhibitor molecules from diverse sources like aristolochic alkaloid, flavonoids and neoflavonoids from plants, hydrocarbones ­2, 4 dimethyl hexane, 2 methylnonane, and 2, 6 dimethyl heptane obtained from traditional medicinal plants Tragia involucrata (Euphorbiaceae) member of natural products involved for the inhibitory potential of phospholipase A(2) (PLA(2)) enzymes in vitro and also decrease both oedema induced by snake venom as well as human synovial fluid PLA(2). Besides marine natural products that inhibit PLA(2) are manoalide and its derivatives such as scalaradial and related compounds, pseudopterosins and vidalols, tetracylne from synthetic chemicals etc. There is an overview of the role of PLA(2) in inflammation that provides a rationale for seeking inhibitors of PLA(2) as anti-inflammatory agents. However, more studies should be considered to evaluate antivenom efficiency of sera and other agents against a variety of snake venoms found in various parts of the world. The implications of these new groups of svPLA(2) toxin inhibitors in the context of our current understanding of snake biology as well as in the development of new novel antivenoms therapeutics agents in the efficient treatment of snake envenomations are discussed. Biomedical Informatics 2012-01-06 /pmc/articles/PMC3282276/ /pubmed/22359435 Text en © 2012 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Current Trends
Perumal Samy, Ramar
Gopalakrishnakone, Ponnampalam
Chow, Vincent TK
Therapeutic application of natural inhibitors against snake venom phospholipase A(2)
title Therapeutic application of natural inhibitors against snake venom phospholipase A(2)
title_full Therapeutic application of natural inhibitors against snake venom phospholipase A(2)
title_fullStr Therapeutic application of natural inhibitors against snake venom phospholipase A(2)
title_full_unstemmed Therapeutic application of natural inhibitors against snake venom phospholipase A(2)
title_short Therapeutic application of natural inhibitors against snake venom phospholipase A(2)
title_sort therapeutic application of natural inhibitors against snake venom phospholipase a(2)
topic Current Trends
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3282276/
https://www.ncbi.nlm.nih.gov/pubmed/22359435
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