Sea snake venoms and neurotoxins

Tu, Anthony T.

doi:10.1021/jf60191a034

Cited by 27 publications

(10 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results might be attributable to the fact that sea snakes contain potent neurotoxins whereas 60% of the protein content in ES venom consists of highly potent postsynaptic neurotoxins (20). It is also important to note that the venoms of sea snakes are characterized by very low levels of enzymatic activities except for PLA 2 and a total lack of L-amino acid oxidase or hemorrhagic activities (21).…”

Section: Discussionmentioning

confidence: 99%

Cytotoxicity of Southeast Asian snake venoms

Jamunaa¹,

Vejayan²,

Halijah³

et al. 2012

J. Venom. Anim. Toxins incl. Trop. Dis

View full text Add to dashboard Cite

Cytotoxicity of venoms from eleven medically important snakes found in Southeast Asia (Naja kaouthia, Naja siamensis, Naja sumatrana, Ophiophagus hannah, Bungarus candidus, Bungarus fasciatus, Enhydrina schistosa, Calloselasma rhodostoma, Trimeresurus purpureomaculatus and Tropidolaemus sumatranus) was determined, based on the MTS cytotoxicity assay, which determines the survival of viable cells in monolayer MDCK and Vero cell cultures upon exposure to the snake venoms. Snake venom toxicity was expressed as the venom dose that killed 50% of the cells (CTC 50 ) under the assay conditions. Venoms of C. rhodostoma (2.6 µg/mL, 1.4 µg/mL) and O. hannah were the most cytotoxic (3.8 µg/mL, 1.7 µg/mL) whereas N. siamensis venom showed the least cytotoxicity (51.9 µg/mL, 45.7 µg/mL) against Vero and MDCK cells, respectively. All the viper venoms showed higher cytotoxic potency towards both Vero and MDCK cell lines, in comparison to krait and cobra venoms. E. schistosa did not cause cytotoxicity towards MDCK or Vero cells at the tested concentrations. The cytotoxicity correlates well with the known differences in the composition of venoms from cobras, kraits, vipers and sea snakes.

show abstract

Section: Discussionmentioning

confidence: 99%

Cytotoxicity of Southeast Asian snake venoms

Jamunaa¹,

Vejayan²,

Halijah³

et al. 2012

J. Venom. Anim. Toxins incl. Trop. Dis

View full text Add to dashboard Cite

show abstract

“…Bioactive peptides were first discovered and isolated in marine species as neurotoxin [ 3 ], cardiotonic peptide [ 4 ], antiviral and antitumor peptide [ 5 ], cardiotoxin [ 6 ] and antimicrobial peptide [ 7 ]. Since then, the investigations on marine bioactive peptides have continued with intent to also ascertain their applications.…”

Section: Introductionmentioning

confidence: 99%

Marine Peptides: Bioactivities and Applications

2015

View full text Add to dashboard Cite

Peptides are important bioactive natural products which are present in many marine species. These marine peptides have high potential nutraceutical and medicinal values because of their broad spectra of bioactivities. Their antimicrobial, antiviral, antitumor, antioxidative, cardioprotective (antihypertensive, antiatherosclerotic and anticoagulant), immunomodulatory, analgesic, anxiolytic anti-diabetic, appetite suppressing and neuroprotective activities have attracted the attention of the pharmaceutical industry, which attempts to design them for use in the treatment or prevention of various diseases. Some marine peptides or their derivatives have high commercial values and had reached the pharmaceutical and nutraceutical markets. A large number of them are already in different phases of the clinical and preclinical pipeline. This review highlights the recent research in marine peptides and the trends and prospects for the future, with special emphasis on nutraceutical and pharmaceutical development into marketed products.

show abstract

“…The venom of sea snakes contains potent neurotoxins which bind to the acetylcholine receptor in the neuromuscular junction [7]. Utilizing this property, many investigators are using snake neurotoxins to elucidate the mechanism of neurotransmission across the synapses or neuromuscular junction.…”

Section: Introductionmentioning

confidence: 99%

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

et al. 2015

View full text Add to dashboard Cite

This study is designed to isolate and purify a novel anti-clotting protein component from the venom of Enhydrina schistosa, and explore its biochemical and biological activities. The active protein was purified from the venom of E. schistosa by ion-exchange chromatography using DEAE-cellulose. The venom protein was tested by various parameters such as, proteolytic, haemolytic, phospholipase and anti-coagulant activities. 80 % purity was obtained in the final stage of purification and the purity level of venom was revealed as a single protein band of about 44 kDa in SDS-polyacrylamide electrophoresis under reducing conditions. The results showed that the Potent hemolytic activity was observed against cow, goat, chicken and human (A, B and O positive) erythrocytes. Furthermore, the clotting assays showed that the venom of E. schistosa significantly prolonged in activated partial thromboplastin time, thrombin time, and prothrombin time. Venomous enzymes which hydrolyzed casein and gelatin substrate were found in this venom protein. Gelatinolytic activity was optimal at pH 5-9 and 1 H NMR analysis of purified venom was the base line information for the structural determination. These results suggested that the E. schistosa venom holds good promise for the development of novel lead compounds for pharmacological applications in near future.

show abstract

Sea snake venoms and neurotoxins

Cited by 27 publications

References 28 publications

Cytotoxicity of Southeast Asian snake venoms

Cytotoxicity of Southeast Asian snake venoms

Marine Peptides: Bioactivities and Applications

RETRACTED ARTICLE: Biological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity

Contact Info

Product

Resources

About