EFFECTS OF DRUGS AGAINST ANTIOXIDANT AND CYTOTOXIC (HEp 2 CELL LINE) ACTIVITY COMPOUNDS FROM MARINE ANIMALS CONUS AMADIS VENOM (GMELIN, J.F, 1791)

Authors

  • Ramesh S. Centre of Advanced Study in Marine Biology, Faculty of Marine Sciences Annamalai University Parangipettai 608502, Tamilnadu, India.
  • E. Dilipan Centre of Advanced Study in Marine Biology, Faculty of Marine Sciences Annamalai University Parangipettai 608502, Tamilnadu, India.
  • P. Mayavu Centre of Advanced Study in Marine Biology, Faculty of Marine Sciences Annamalai University Parangipettai 608502, Tamilnadu, India.

Keywords:

Gastropod, Conus amadis, Venom gland, Antioxidant and HEp-2 Cell line and MTT assay

Abstract

Objective: The present study was carried out to explore the hemolytic, antioxidant and cytotoxic activity of conotoxins extracted from the venom of C. amadis.

Methods: The crude conotoxin was extracted and tested for cytotoxic, antioxidant activity and cancer cell lines. The cytotoxic activity was studied by brine shrimp cells and in-vitro antioxidant activity were determined by DPPH, Superoxide anion radical scavenging assay and hydrogen peroxide scavenging from active fraction of conopeptides. The active fractions were tested in HEp-2 cancer cell lines at different concentration.

Results: The different dose tested viz 100μg/mL-1, 50μg/mL-1, 25μg/mL-1, 12.5μg/mL-1, 6.25μg/mL-1, and 3.2μg/mL-1 cytotoxicity on HEp-2 cell was observed at the 25μg/mL. HEp-2 cell displayed dose dependent decreased in viability detected as early as 48 hrs. The purified conotoxin was showed remarkable cytotoxicity against HEp-2 cell in a dose depend manner. The isolated conotoxin that produced maximum effect at 100μg/mL-1 and the half inhibitory concentrations (IC50) was 25μg/mL-1 in the concentration of 45.6±0.8%.

Conclusion: The present study revealed that cono-peptides from C. amadis have been used as an accessible source of natural antioxidants as well as anticancer after trial with animal and pre-clinical studies.

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References

Sies H, J. Strategies of antioxidant defense. J Eur 1999;215(2):213-9.

Yang CS, Landau JM, Huang MT, Newmark HL. Inhibition of carcinogenesis by dietary polyphenolic compounds. J Annu Rev Nutr 2001;21:381-406.

Castenga A, Pocernich CB, Drake J, Scapagnini G, Calabrese V, J. Butterï¬eld DA. Nutritional approaches to combat oxidative stress in Alzheimers disease. J Nut Biochem 2002;13:444-61.

Frlich I, Riederer P. Free radical mechanisms in dementia of Alzheimer type and the potential for antioxidative treatment. J Drug Res 1995;45:443-9.

Kim SK., Jeon YJ., Byun HG. and Park PJ. Calcium absorption acceleration effect on phosphorylated and nonphosphorylated peptides from hoki Johnius belengeri frame. J Korean Fish Soc 1999;32:713–7.

Aruoma IO, J. Free radicals, oxidative stress and antioxidants in human health and disease. J Oil Chem Soc 1998;75:199-212.

Amarowicz R, Shahidi F. Antioxidant activity of peptide fractions of capelin protein hydrolysates. J Food Chem 1997;58:355-9.

Aluko RE, Monu E, J. Functional and bioactive properties of quinoa seed protein hydrolysates. J Sci 2003;68:1254-8.

Cumby N, Zhong Y, Naczk M, Shahidi F. Antioxidant activity and water-holding capacity of canola protein hydrolysates. J Food Chem 2008;109:144-8.

Sakanaka S, Tachibana Y, Ishihara N, Juneja LR. Antioxidant activity of egg-yolk protein hydrolysates in a linoleic acid oxidation system. J Food Chem 2004;86:99-103.

Blanca HL, Ana Q, Lourdes A, Isidra R, Dairy J. and Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin. J Int 2007;17:42-9.

Kim S-Y, Je J-Y, Kim S-K. Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. J of Nutritional Biochemistry 2007;18(1):31-8.

Wu HC., Chen HM. and Shiau CY. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel Scomber austriasicus. J Food Res Int 2003;10:949-57.

Pihlanto-Leppala A. Bioactive peptides derived from bovine proteins:opioid and ACE-inhibitory peptides. J Trend Food Sci Technol 2001;11:347-56.

Fry BG, Roelants K, Champagne DE, Scheib H, Tyndall JDA, King GF, et al. The toxicogenomic multiverse :convergent recruitment of proteins into animal venoms. J Annual Review of Genomics and Human Genetics 2009;10:483-511.

McManus OB, Musick JR, Gonzalez C. and Peptides isolated from the venom of Conus geographus block neuromuscular transmission. J Neurosci Lett 1987;7(25):57-62.

Lewis RJ. Conotoxin venom peptide therapeutics. J Advan Exper Med Biol 2009;55:44-8.

Saravanan R., Sambasivam S., Shanmugam A., Sathishkumar D., Tamilvannan T. and Nazeer RA., (2009) Isolation, purification and biochemical characterization of conotoxin from Conus fugulinus (1758). Indian J Biotechnol 1758;8:266-71.

McIntosh JM, Ghomashchi F, Gelb MH, Dooley DJ, Stoehr SJ, Giordani AB, et al. Conodipine-M, a novel phospholipase A2 isolated from the venom of the marine snail Conus magus. J of Biological Chemistry 1995;270(8):3518-26.

Nenadis N, Tsimidou SJ, J. Observations on the estimation of scavenging activity of phenolic compounds using rapid 1-diphenyl2-picrylhydrazyl (DPPH) tests. J Oil Chem Soc 79 2002;1:1191-5.

Nishikimi M, Kawai T, Yagi K. Guinea pigs possess a highly mutated gene for L-gulono-gamma-lactone oxidase, the key enzyme for L-ascorbic acid biosynthesis missing in this species. J of Biological Chemistry 1992;267(30):21967-72.

Klein SM, Cohen G, Cederbaum AI. Production of formaldehyde during metabolism of dimethyl sulfoxide by hydroxyl radical generating systems. J Biochemistry 1981;20(21):6006-12.

Meyer BN, Ferrigni NR, Putnam JE, Jacobsen LB, Nichols DE, McLaughlin JL. Brine shrimp:a convenient general bioassay for active plant constituents. J Planta Med 1982;45(5):31-4.

Finney DJ. Probit Analysis. 3rd ed. Cambridge University press:Cambridge, London;1971.

Mosmann T. Rapid colorimetric assay for cellular growth and survival:application to proliferation and cytotoxicity assays. J Immunol Methods 1983;65(1-2):55-63.

Blanchfield JT, Dutton JL, Hogg RC, Gallagher OP, Craik DJ, Jones A, et al. Synthesis, structure elucidation, in vitro biological activity, toxicity, and Caco-2 cell permeability of lipophilic analogues of alpha-conotoxin MII. J Med Chem 2003;46(7):1266-72.

Sivaperumal P, Kamala K, Natarajan E, Dilipan E, J. Antimicrobial peptide from crab haemolypmh of Ocypoda macrocera (Milne Edwards with reference to antioxidant:a case study. J Int Pharm Sci 1852;5(2):719-27.

Li H, Liu BL, Gao LZ, Chen HL. and, Study on bullfrog skin collagen. J Food Chem 2004;84:65-9.

Jun SY, Park PJ, Jung WK, Kim SK. and, Puriï¬cation and characterization of an antioxidative peptide from enzymatic hydrolysate of yellow ï¬n sole (Limanda aspera) frame protein. J Eur Food Res Technol 2004;219:20-6.

Prathapan A, Singh MK, Anusree SS, Kumar DR, Raghu KG, Sundaresan A, et al. and, Antiperoxidative, free radical scavenging and metal chelating activities of Boerhaavia diffusa. J Biochem 2010;35(5):1548-54.

Ilhami G, Alici H, Cesur M. Ahmet and Determination of in vitro antioxidant and radical scavenging activities of propofol. J Chem Pharm Bull 2005;53:281-5.

Abdel-Rahman MA, Omran MAA, Abdel-Nabi IM, Nassier OA, Schemerhorn BJ. Neurotoxic and cytotoxic effects of venom from different populations of the Egyptian Scorpio maurus palmatus. Toxicon:official J of the Int Soc on Toxinology 2010;55(2-3):298-306.

Aurand LW, Oonem NH, Gidding GG, J. and, Superoxide and singlet oxygen in mill lipid peroxidation. J Sci 1977;60:363-9.

Bhavani B, Pogozelski WK, Tullius WK. DNA strand breaking by hydroxyl radical is governed by the accessible surface area of the hydrogen atoms of the DNA backbones. J Proc National Acad Sci 1998;95:9738-43.

Kawsar SMA, Mamun SMA, Rahman MS, Yasumitsu H, Ozeki Y. and. Growth inhibitory effects on microorganisms by a D-galactose-binding lectin purified from the sea hare (Aplysia kurodai) eggs:An in vitro study. J Nat Sci 2010;8:82-9.

Ganassin RC, Bols NC, Schirmer K, Ostrander GK. J Cell and Tissue Culture 2000;631-51.

Bilberg K, Hovgaard MB, Besenbacher F, Baatrup E. In Vivo Toxicity of Silver Nanoparticles and Silver Ions in Zebrafish (Danio rerio). J Toxicol 2012;2012:293784

Published

01-07-2014

How to Cite

S., R., E. Dilipan, and P. Mayavu. “EFFECTS OF DRUGS AGAINST ANTIOXIDANT AND CYTOTOXIC (HEp 2 CELL LINE) ACTIVITY COMPOUNDS FROM MARINE ANIMALS CONUS AMADIS VENOM (GMELIN, J.F, 1791)”. International Journal of Pharmacy and Pharmaceutical Sciences, vol. 6, no. 7, July 2014, pp. 638-43, https://journals.innovareacademics.in/index.php/ijpps/article/view/2416.

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