In vitro screening and evaluation of antivenom phytochemicals from Azima tetracantha Lam. leaves against Bungarus caeruleus and Vipera russelli

Janardhan, Bhavya; Shrikanth, Vineetha M.; Mirajkar, Kiran K.; More, Sunil S.

doi:10.1186/1678-9199-20-12

Cited by 23 publications

(16 citation statements)

References 24 publications

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“…Additionally, the LAAOs of Naja naja kaouthia and Calloselasma rhodostoma venoms were inhibited by polyphenols from Areca catechu and Quercus infectoria extracts evaluated by in vitro tests [ 28 ]. Although the ethylacetate extract from Azima tetracantha leaves exerts an in vitro inhibitory activity on toxic enzymes from B. caeruleus and Vipera russelli venoms, LAAOs from neither venom was inhibited [ 29 ].…”

Section: Introductionmentioning

confidence: 99%

Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

Bordon¹,

Wiezel²,

Cabral³

et al. 2015

J Venom Anim Toxins Incl Trop Dis

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BackgroundCrotalus durissus terrificus venom (CdtV) is one of the most studied snake venoms in Brazil. Despite presenting several well known proteins, its L-amino acid oxidase (LAAO) has not been studied previously. This study aimed to isolate, characterize and evaluate the enzyme stability of bordonein-L, an LAAO from CdtV.MethodsThe enzyme was isolated through cation exchange, gel filtration and affinity chromatography, followed by a reversed-phase fast protein liquid chromatography to confirm its purity. Subsequently, its N-terminal amino acid sequence was determined by Edman degradation. The enzyme activity and stability were evaluated by a microplate colorimetric assay and the molecular mass was estimated by SDS-PAGE using periodic acid-Schiff staining and determined by mass spectrometry.ResultsThe first 39 N-terminal amino acid residues exhibited high identity with other snake venom L-amino acid oxidases. Bordonein-L is a homodimer glycoprotein of approximately 101 kDa evaluated by gel filtration. Its monomer presents around 53 kDa estimated by SDS-PAGE and 58,702 Da determined by MALDI-TOF mass spectrometry. The enzyme exhibited maximum activity at pH 7.0 and lost about 50 % of its activity after five days of storage at 4 °C. Bordonein-L’s activity was higher than the control when stored in 2.8 % mannitol or 8.5 % sucrose.ConclusionsThis research is pioneering in its isolation, characterization and enzyme stability evaluation of an LAAO from CdtV, denominated bordonein-L. These results are important because they increase the knowledge about stabilization of LAAOs, aiming to increase their shelf life. Since the maintenance of enzymatic activity after long periods of storage is essential to enable their biotechnological use as well as their functional studies.

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Section: Introductionmentioning

confidence: 99%

Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

Bordon¹,

Wiezel²,

Cabral³

et al. 2015

J Venom Anim Toxins Incl Trop Dis

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“…Similarly, methanolic extract of L. aspera has shown inhibitory action on protease activity of cobra venom [ 35 ]. Janardhan, B. et al (2014) studied the antivenom activity of extract isolated from A. etracantha leaves against viper venom and krait, where they observed inhibitory activity on phospholipases, phospholdiesterase while no inhibitory activity on protease observed [ 19 ].…”

Section: Resultsmentioning

confidence: 99%

“…L-tyrosine was used as a standard. One unit of enzyme activity was defined as the amount that yielded 0.02 μmole of tyrosine/ hour [ 19 ]. The same experiment was performed for the samples by pre-incubating venom (20 μg–100 μg) with varying concentrations of SNPs (0.062 nM, 0.124 nM, 0.186 nM, 0.248 nM SNP).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of crude viper venom action by silver nanoparticles: A biophysical and biochemical study

2018

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This investigation understands the interaction between lyophilized crude Viper snake venom (Doboia russellie) and Silver nanoparticles (SNPs) using biophysical and biochemical approaches. SNPs were synthesized by chemical reduction method and characterized using UV-Visible spectroscopy, Dynamic Light Scattering (DLS) and Transmission electron microscope (TEM). The average hydrodynamic size of SNPs was found to be 52 nm with 0.261 PDI. TEM image revealed the spherical shape of SNP. Interaction of SNPs and viper venom was resulted in the formation of complex which was confirmed by using DLS technique. Spectroscopic results showed an increase in absorbance intensity of venom upon interaction with SNPs which indicated interaction with venom proteins. Fluorescence spectroscopic data revealed the quenching in the fluorescence intensity of viper venom upon incubation with varying concentration of SNPs. The results obtained by biochemical assays (Protease and whole blood clotting test) revealed the inhibition of venom action due to presence of silver nanoparticles. The activity of protease enzyme was found to be decreased (10–13% reduction) in presence of silver nanoparticles. Prolonged clotting time (two fold) of viper venom upon interaction with SNPs compared to native crude viper venom was observed. The overall results confirmed the inhibition action of silver nanoparticles against viper venom.

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“…Various plants have been studied for inhibition of these toxic enzymes effects by in vitro using various solvent extracts. In vitro inhibitory activity of Carissa spinarum leaf extracts against Krait and Viper russellitoxic snake venom enzymes was studied (Janardhan et al, 2014). Tabernaemontana alternifolia inhibits in vitro N. naja and E. carinatus venom enzyme activities (Vineetha et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

In vitro neutralization of Eachis carinatus and Naja naja venom by Canthium parviflorum and its GC-MS analysis

Shrikanth

Janardhan

2016

Bangladesh J Pharmacol

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Canthium parviflorum is used in the traditional therapy to treat snakebite victims. In the present study, partially purified methanol root extract of C. parviflorum was used for the neutralization of Eachis carinatus and Naja naja venom. The extract inhibited in vitro phosphomonoesterase, phosphodiesterase, acetylcholinesterase, hyaluronidase, protease, phospholipase A2 and 5’nucleotidase activities of both venoms. One of the promising band exhibited neutralization of all the in vitro enzyme activities and was further subjected to GC-MS analysis which revealed the presence of eight active phytocompounds. These phytochemicals might be responsible for in vitro enzyme neutralization. Methanol extract possesses potent active phytochemicals against the site specific toxins and hydrolytic enzymes analyzed.Video Clip of Methodology:<a href="https://youtube.com/v/oSLdFcfaJxU">Phospholipase A2 assay</a>: 1 min 36 sec

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In vitro screening and evaluation of antivenom phytochemicals from Azima tetracantha Lam. leaves against Bungarus caeruleus and Vipera russelli

Cited by 23 publications

References 24 publications

Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

Inhibition of crude viper venom action by silver nanoparticles: A biophysical and biochemical study

<i>In vitro</i> neutralization of <i>Eachis carinatus</i> and <i>Naja naja</i> venom by <i>Canthium parviflorum</i> and its GC-MS analysis

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