ВЗАИМОДЕЙСТВИЕ ГЛИФОСАТА С АМИНОКИСЛОТАМИ ГЕНЕТИЧЕСКИ МОДИФИЦИРОВАННОЙ РАУНДАПОУСТОЙЧИВОЙ И НЕ ГЕНЕТИЧЕСКИ МОДИФИЦИРОВАННОЙ СОИ В ВОДНОМ РАСТВОРЕ В УСЛОВИЯХ IN VITRO

Кулик Я. М., Обертюх Ю. В., Выговская И. А., Гончар Л. А.

БИОЛОГИЯ

Научная статья.

Установлено, что действующее вещество Roundup – глифосат в условиях in vitro вступает во взаимодействие с ароматическими аминокислотами сои, а с другими аминокислотами в организме, как аналог глицина, образует пептидные соединения, что является подтверждением образования в организме людей и животных неестественных пептидов при наличии в продуктах питания и кормах глифосата.

генетически модифицированная соя, не генетически модифицированная соя, во-дная вытяжка сои, глифосат, Roundup, реакция Паули, формольное титрование

1. Hyl MI, Smetana OY, Yulevych OI, Barkar YV, Horbatenko IY, Nezhlukchenko TI, ta in. Molekuliarna henetyka ta tekhnolohii doslidzhennia henoma: navch. posib. Editor professor MI. Hyl. Kherson: OLDI-PLIUS; 2015. 320 s. [in Ukrainian].
2. Ermakova IV. Geneticheski modifitsirovannaya soya privodit k snizheniyu vesa i uvelicheniyu smertnosti kryisyat pervogo pokoleniya. Predvaritelnyie issledovaniya. Ekoinform. 2006;1. [in Russiаn].
3. Ermakova IV, Barskov IV. Izuchenie fiziologicheskih i morfologicheskih parametrov u kryis i ih potomstva pri ispolzovanii dietyi soderzhaschey soyu s transgenom EPSPS SR4. Modern problems of science and education. Biological Sciences. 2008;6:19-20. [in Russiаn].
4. Ermakova IV. Vliyanie soi s genom EPSPS SR4 na fiziologicheskoe sostoyanie i reproduktivnyie funktsii kryis v pervyih dvuh pokoleniyah. Modern problems of science and education. 2009;5:15-21. [in Russiаn].
5. Ivankin AN, Kulikovskiy AV, Proshina OP. Osnovyi biotehnologii. Laboratornyie rabotyi: ucheb.-metodich. posobie. M.: FGBOU VPO MGUL; 2016. 20 s. [in Russiаn].
6. Kulyk MF, Korniichuk OV, Buhaiov VD, Obertiukh YV, Khimich OV, Lilyk TV, ta in. Pryhnichennia rostu prorostkiv zerna pshenytsi, trytykale i zhyta pid vplyvom vodnoi vytiazhky raundapostiikoi HM soi porivniano z ne HM soieiu. Bulletin of Agrarian Science. 2013;6:21-4. [in Ukrainian].
7. Malyigin AG. Vliyanie soevoy dietyi na reproduktivnyie funktsii myishey. Sovremennyye problemy nauki i obrazovaniya. Biologicheskiye nauki. 2008;6:23. [in Russiаn].
8. Malyigin AG, Ermakova IV. Soevaya dieta podavlyaet reproduktivnyie funktsii gryizunov. Sovremennyye problemy nauki i obrazovaniya. Biologicheskiye nauki. 2008;6:26. [in Russiаn].
9. Margolina A. Pravda i vyimyisel o fitoestrogenah. Nauka i zhizn’. 2008;5:64-72. Available from: https://www.nkj.ru/archive/articles/13952. [in Russiаn].
10. Sahno LO, Komarnitskiy IK, Kuchuk MV. Stiykist do glifosatu i glyufozinatu v pokolinnyah T1–T2 biotehnologichnih roslin ripaku (Brassica napus L.). Visnyk Ukrayinsʹkoho tovarystva henetykiv i selektsioneriv. 2015;13(1):3-10. Available from: http://nbuv.gov.ua/UJRN/Vutgis_2015_13_1_3. [in Ukrainian].
11. Chub VV. Rasteniya-GMO: kak eto delaetsya. Potentsial. Khimiya. Biologiya. Meditsina. 2011;11:11. Available from: http://elementy.ru/nauchno-populyarnaya_biblioteka/431512/Rasteniya_GMO_kak_eto_delaetsya. [in Russiаn].
12. Amrhein N, Deus B, Gehrke P, Steinrücken HC. The site of the inhibition of the shikimate pathway by glyphosate, II: interference of glyphosate with chorismate formation in vivo and in vitro. Plant Physiol. 1980;66(5):830-4.
13. Coullery RP, Ferrari ME, Rosso SB. Neuronal development and axon growth are altered by glyphosate through a WNT non-canonical signaling pathway. Neurotoxicology. 2015;52:150-61.
14. Florio T, Paludi D, Villa V, et al. Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic. J. Neurochem. 2003;85:62-72.
15. Handel CM, Pajot LM, Matsuoka SM, et al. Epizootic of beak deformities among wild birds in Alaska: An emerging disease in North America? Auk. 2010;127:882-98.
16. Handel CM, Van Hemert C. Environmental contaminants and chromosomal damage associated with beak deformities in a resident North American passerine. Environ. Toxicol. Chem. 2015;34:314-27.
17. Harrison CF, Lawson VA, Coleman BM,et al. Conservation of a glycine-rich region in the prion protein is required for uptake of prion infectivity. J. Biol. Chem. 2010;285:20213-23.
18. Howe RK, Chott RC, McClanahan RH.The Metabolism of Glyphosate in Sprague Dawley Rats. Part II. Identification, Characterization and Quantification of Glyphosate and its Metabolites after Intravenous and Oral Administration (unpublished study MSL-7206 conducted by Monsanto and submitted to the EPA July 1988).
19. Ma Q. Role of Nrf2 in oxidative stress and toxicity. A. Rev. Pharmacol. Toxicol. 2013;53:401-26.
20. Ogura T, Tong KI, Mio K. Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains. Proc. Natl Acad. Sci. USA. 2010;107:2842-7.
21. Rymer D, Good TA. The role of prion peptide structure and aggregation in toxicity and membrane binding. J. Neurochem. 2000;75:2536-45.
22. Samsel A, Seneff S. Glyphosate pathways to modern diseases V: Amino acid analogue of glycine in diverse proteins. Journal of Biological Physics and Chemistry. 2016;16:9-46.
23. Suzuki T, Maher J, Yamamoto M. Select heterozygous Keap1 mutations have a dominant-negative effect on wildtype keap1 in vivo. Cancer Res. 2010;71:1700-9.
24. Tagliavini F, Prelli F, Verga L, et al. Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro. Proc. Natl Acad. Sci. USA. 1993;90:9678-82.

«Вестник проблем биологии и медицины» Выпуск 1 Том 1 (142), 2018 год, 73-78 страницы, код УДК 604:633.34:632.954

10.29254/2077-4214-2018-1-1-142-73-78