СПЕКТРОСКОПІЧНЕ ВИВЧЕННЯ ВЗАЄМОДІЇ ДОЛУТЕГРАВІРУ НАТРІЮ З СИРОВАТКОВИМ АЛЬБУМІНОМ ЛЮДИНИ

A. V. Yegorova, G. V. Maltsev, Yu. V. Scrypynets, S.N. Kashutskуy, V. P. Antonovich

Анотація


Досліджено взаємодію між долутегравіром натрію (ДН) і сироватковим альбуміном людини (САЛ) методом флуоресценції в поєднанні з методом ультрафіолетової спектроскопії в модельних фізіологічних умовах. Результати експерименту показують, що ДН гасить власну флуоресценцію білка в результаті статичної взаємодії в системі САЛ-ДН, що підтверджується зсувами в разностних УФ-спектрах САЛ-ДН і зменшенням константи зв’язування для системи САЛ-ДН з підвищенням температури. Встановлено константу та число місць зв’язування системи САЛ-ДН. Відповідно до теорії резонансного переносу енергії, встановлено, що середня відстань між донорними і акцепторними молекулами для системи САЛ-ДН становить 2,14 нм.


Ключові слова


сироватковий альбумін людини, флуоресценція, долутегравір натрію

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PDF (Русский)

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Gentili P.L., Ortica F., Favaro G. Static and Dynamic Interaction of a Naturally Occurring Photochromic Molecule with Bovine Serum Albumin Studied by UV-Visible Absorption and Fluorescence Spectroscopy. J. Phys. Chem. B, 2008, vol. 112, рр. 16793-16801. http://dx.doi.org/10.1021/jp805922g

Tian J.N., Liu J.Q., He W., Hu Z.O., Yao X.J., Chen X.G. Probing the Binding of Scutellarin to Human Serum Albumin by Circular Dichroism, Fluorescence Spectroscopy, FTIR and Molecular Modeling Method. Biomacromolecules, 2004, vol. 5, рр. 1956-1961. http://dx.doi.org/10.1021/bm049668m

Peters T. All about Albumin: Biochemistry, Genetics, and Medical Applications. Academic Press, San Diego, CA, USA, 1996, 432 p.

Kwon S., Carson J.H. Fluorescence Quenching and Dequenching Analysis of RNA Interactions in Vitro and in Vivo. Anal. Biochem., 1998, vol. 264, рр. 133-140. http://dx.doi.org/10.1006/abio.1998.2846

Khan S.N., Islam B., Yennamalli R., Sultan A., Subbarao N., Khan A.U. Interaction of mitoxantrone with human serum albumin: Spectroscopic and molecular modeling studies. Europ. J. Pharm. Sci., 2008, vol. 35, no 5, pp. 371-382. http://dx.doi.org/10.1016/j.ejps.2008.07.010

Wang Y., Tang B., Zhang H., Zhou Q., Zhang G. Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach. J. Photochem. Photobiol. B: Biology, 2009, vol. 94, рр. 183–190. https://doi.org/10.1016/j.jphotobiol.2008.11.013

Gao X., Tang Y., Rong W., Zhang X., Zhao W., Zi Y. Analysis of binding interaction between captopril and human serum albumin. Amer. J. Anal. Chem., 2011, vol. 2, рр. 250-257. http://dx.doi.org/10.4236/ajac.2011.22030

Roy S., Ganai S., Nandi R.K., Majundar K.C., Das T.K. Studies of the interaction of bovine serum albumin with pyrimidine-annulated spirodihydrofuran and its biological activities. Adv. Mater. Lett., 2015, vol. 6, no 11, рр. 1018-1024. http://dx.doi.org/10.5185/amlett.2015.5933

Xu H., Yao N., Xu H., Wang T., Li G., Li Z. Characterization of the interaction between eupatorin and bovine serum albumin by spectroscopic and molecular modeling methods. Int. J. Mol. Sci., 2013, vol. 14, рр. 14185- 14203. http://dx.doi.org/10.3390/ijms140714185

Rasoulzadeh F., Asgari D., Naseri A., Rashidi M.R. Spectroscopic studies on the interaction between erlotinib hydrochloride and bovine serum albumin. DARU, 2010, vol. 18, рр. 179-184.

Hossain M., Khan A.Y., Kumar G.S. Interaction of the anticancer plant alkaloid sanguinarine with bovine serum albumin. PLOS One. 2011, vol. 6, no 4, рр. e18333. https://doi.org/10.1371/journal.pone.0018333

Wang C., Wu Q.-H., Wang Z., Zhao J. Study of the interaction of carbamazepine with bovine serum albumin by fluorescence quenching method. Anal. Sci., 2006, vol. 22, рр. 435-438. https://www.jstage.jst.go.jp/article/ analsci/22/3/22_3_435/_pdf

Roy A.S., Tripathy D.R., Chatterjee A., Dasgupta S. A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin. J. Biophys. Chem., 2010, vol. 1, рр. 141-152. doi:10.4236/jbpc.2010.13017

Varlan A., Hillebrand M. Bovine and human serum albumin interactions with 3-carboxyphenoxathiin studied by fluorescence and circular dichroism spectroscopy. Molecules, 2010, vol. 15, рр. 3905-3919. doi:10.3390/ molecules15063905

Dong S., Li Z., Shi L., Huang G., Chen S., Huang T. The interaction of plant-growth regulators with serum albumin: Molecular modeling and spectroscopic methods. Food Chem. Toxicol., 2014, vol. 67, рр. 123–130. http://dx.doi.org/10.1016/j.fct.2014.02.020

Jin J., Zhang X. Spectrophotometric studies on the interaction between pazufloxacin mesilate and human serum albumin or lysozyme. J. Lumin., 2008, vol. 128, рр. 81–86. http://dx.doi.org/10.1016/j.jlumin.2007.05.008

Zhang H.M., Wangn Y.Q., Zhou Q.H. Fluorimetric study of interaction of benzidine with trypsin. J. Lumin., 2010, vol. 130, рр. 781–786. http://dx.doi.org/10.1016/j.jlumin.2009.11.032

Li D., Zhu J., Jin J. Spectrophotometric studies on the interaction between nevadensin and lysozyme. J. Photochem. Photobiol. A: Chemistry, 2007, vol. 189, рр. 114–120. http://dx.doi.org/10.1016/j.jphotochem. 2007.01.017

Zhu J., Li D., Jin J., Wu L. Binding analysis of farrerol to lysozyme by spectroscopic methods. Spectrochim. Acta Part A, 2007, vol. 68, рр. 354–359. http://dx.doi.org/10.1016/j.saa.2006.11.045

Gowda B., Mallappa M., Gowda J., Rengasamy R. Interaction of ketoconazole with bovine serum albumin: electrochemical, spectroscopic and molecular modeling studies. J. Appl. Pharm. Sci., 2015, vol. 5, рр. 037-044. http://dx.doi.org/10.7324/JAPS.2015.58.S6

Abu Teir M.M., Ghithan J., Abu-Taha M.I., Darwish S.M., Abu-hadid M.M. Spectroscopic approach of the interaction study of ceftriaxone and human serum albumin. J. Biophys. Struct. Biol., 2014, vol. 6, рр. 1-12. http:// dx.doi.org/10.5897/JBSB2013.0045

Hamdi O., Feroz S., Shilpi J., Anouar El. H., Mukarram A., Mohamad S.B., Tayyab S., Awang K. Spectrofluorometric and molecular docking studies on the binding of curcumenol and curcumenone to human serum albumin. Int. J. Mol. Sci., 2015, vol. 16, рр. 5180-5193. http://dx.doi.org/10.3390/ijms16035180

Salam M.A., Rokonujjaman M., Rahman A., Sultana U.N., Zakir S.M. Study of in Vitro Interaction of Sildenafil Citrate with Bovine Serum Albumin by Fluorescence Spectroscopy. Pharmacology Pharmacy, 2015, vol. 6, no 2, рр. 94-101. http://dx.doi.org/10.4236/pp.2015.62012

Meti M.D., Nandibewoor S.T., Joshi S.D., More U.A., Chimatadar S.A. Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin. J. Pharm. Anal., 2015, vol. 5, рр. 249–255. http:// dx.doi.org/10.1016/j.jpha.2015.01.004

Naik P.N., Nandibewoor S.T., Chimatadar S.A. Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling. J. Pharm. Anal., 2015, vol. 5, рр. 143–152. http://dx.doi.org/10.1016/j.jpha.2015.01.003

Khan S.N., Islam B., Khan A.U. Probing midazolam interaction with human serum albumin and its effect on structural state of protein. Int. J. Integ. Biol., 2007, vol. 1, рр. 102–112.

Valeur B., Brochon J.C. New Trends in Fluorescence Spectroscopy 6th edn (Berlin : Springer), 1999, pp. 25–28.

Lakowicz J.R. Principles of Fluorescence Spectroscopy. 3rd edn. New York:Springer, 2006, 954 p.

Sahoo B.K., Ghosh K.S., Dasgupta S. Molecular interactions of isoxazolcurcumin with human serum albumin: Spectroscopic and molecular modeling studies. Biopolymers, 2009, vol. 91, рр. 108–119. http://dx.doi. org/10.1002/bip.21092

Silva D., Cortez C.M., Cunha-Bastos J., Louro S.R.W. Methyl parathion interaction with human and bovine serum albumin. Toxicol. Lett., 2004, vol. 147, рр. 53–61. http://dx.doi.org/10.1016/j.toxlet.2003.10.014

Ross P. D., Subramanian S. Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 1981, vol. 20, рр. 3096–3102. http://dx.doi.org/10.1021/bi00514a017

Aki H., Yamamoto M. Thermodynamics of the binding of phenothiazines to human plasma, human serum albumin and alpha 1-acid glycoprotein: a calorimetric study. J. Pharm. Pharmacol., 1989, vol. 41, рр. 674-679. http://dx.doi.org/10.1111/j.2042-7158.1989.tb06339.x

Miller J.N. Recent advances in molecular luminescence analysis. Proc. Anal. Div. Chem. Soc., 1979, vol. 16, no. 7, рр. 203–208.

Wu P., Brand L. Resonance energy transfer: Methods and applications. Anal. Biochem., 1994, vol. 218, рр. 1–13.

Forster T. Zwischenmolekulare energiewanderung und fluoreszenz. Ann. Phys., 1948, vol. 2, рр. 55–75.

Xiao J.B., Shi J., Cao H., Wu S.D., Ren F.L., Xu M. Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method. J. Pharm. Biomed. Anal., 2007, vol. 45, рр. 609–615. http:// dx.doi.org/10.1016/j.jpba.2007.08.032.


Пристатейна бібліографія ГОСТ


1. Gentili P.L., Ortica F., Favaro G. Static and Dynamic Interaction of a Naturally Occurring Photochromic Molecule with Bovine Serum Albumin Studied by UV-Visible Absorption and Fluorescence Spectroscopy // J. Phys. Chem. B. – 2008. – Vol. 112. – P. 16793-16801. http://dx.doi.org/10.1021/jp805922g

2. Tian J.N., Liu J.Q., He W., Hu Z.O., Yao X.J., Chen X.G. Probing the Binding of Scutellarin to Human Serum Albumin by Circular Dichroism, Fluorescence Spectroscopy, FTIR and Molecular Modeling Method // Biomacromolecules – 2004. – Vol. 5. – P. 1956-1961. http://dx.doi.org/10.1021/bm049668m

3. Peters T. All about Albumin: Biochemistry, Genetics, and Medical Applications; Academic Press: San Diego, CA, USA. – 1996. – 432 p.

4. Kwon S., Carson J.H. Fluorescence Quenching and Dequenching Analysis of RNA Interactions in Vitro and in Vivo // Anal. Biochem. – 1998. – Vol. 264. – P. 133-140. http://dx.doi.org/10.1006/abio.1998.2846

5. Khan S.N., Islam B., Yennamalli R., Sultan A., Subbarao N., Khan A.U. Interaction of mitoxantrone with human serum albumin: Spectroscopic and molecular modeling studies // Еurop. J. Pharm. Sci. – 2008. – Vol. 35. – P. 371–382. http://dx.doi.org/10.1016/j.ejps.2008.07.010

6. Wang Y., Tang B., Zhang H., Zhou Q., Zhang G. Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach // J. Photochem. Photobiol. B: Biology – 2009. – Vol. 94. – P. 183–190. https://doi.org/10.1016/j.jphotobiol.2008.11.013

7. Gao X., Tang Y., Rong W., Zhang X., Zhao W., Zi Y. Analysis of binding interaction between captopril and human serum albumin // Amer. J. Anal. Chem. –2011. – Vol. 2. – P. 250-257. http://dx.doi.org/10.4236/ajac.2011.22030

8. Roy S., Ganai S., Nandi R.K., Majundar K.C., Das T.K. Studies of the interaction of bovine serum albumin with pyrimidine-annulated spirodihydrofuran and its biological activities // Adv. Mater. Lett. – 2015. – Vol. 6, No11. – P. 1018-1024. http://dx.doi.org/10.5185/amlett.2015.5933

9. Xu H., Yao N., Xu H., Wang T., Li G., Li Z. Characterization of the interaction between eupatorin and bovine serum albumin by spectroscopic and molecular modeling methods // Int. J. Mol. Sci. – 2013. – Vol. 14. – P. 14185-14203. http://dx.doi.org/10.3390/ijms140714185

10. Rasoulzadeh F., Asgari D., Naseri A., Rashidi M.R. Spectroscopic studies on the interaction between erlotinib hydrochloride and bovine serum albumin // DARU – 2010. – Vol. 18. – P. 179-184.

11. Hossain M., Khan A.Y., Kumar G.S. Interaction of the anticancer plant alkaloid sanguinarine with bovine serum albumin. PLOS One // 2011. – Vol. 6, No 4. –P. e18333. https://doi.org/10.1371/journal.pone.0018333

12. Wang C., Wu Q.-H., Wang Z., Zhao J. Study of the interaction of carbamazepine with bovine serum albumin by fluorescence quenching method // Anal. Sci. – 2006. – Vol. 22. – P. 435-438. https://www.jstage.jst.go.jp/ article/analsci/22/3/22_3_435/_pdf

13. Roy A.S., Tripathy D.R., Chatterjee A., Dasgupta S. A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin // J. Biophys. Chem. – 2010. – Vol. 1. – P. 141-152. http://dx.doi. org/10.4236/jbpc.2010.13017

14. Varlan A., Hillebrand M. Bovine and human serum albumin interactions with 3-carboxyphenoxathiin studied by fluorescence and circular dichroism spectroscopy // Molecules – 2010. – Vol. 15. – P. 3905-3919. http://dx.doi. org/10.3390/molecules15063905

15. Dong S., Li Z., Shi L., Huang G., Chen S., Huang T. The interaction of plant-growth regulators with serum albumin: Molecular modeling and spectroscopic methods // Food Chem. Toxicol. – 2014. – Vol. 67. – P. 123–130. http://dx.doi.org/10.1016/j.fct.2014.02.020

16. Jin J., Zhang X. Spectrophotometric studies on the interaction between pazufloxacin mesilate and human serum albumin or lysozyme // J. Lumin. – 2008. – Vol. 128. – P. 81–86. http://dx.doi.org/10.1016/j.jlumin.2007.05.008

17. Zhang H.M., Wangn Y.Q., Zhou Q.H. Fluorimetric study of interaction of benzidine with trypsin // J. Lumin. – 2010. – Vol. 130. – P. 781–786. http://dx.doi.org/10.1016/j.jlumin.2009.11.032

18. Li D., Zhu J., Jin J. Spectrophotometric studies on the interaction between nevadensin and lysozyme // J. Photochem. Photobiol. A: Chemistry – 2007. – Vol. 189. – P. 114–120. http://dx.doi.org/10.1016/j.jphotochem. 2007.01.017

19. Zhu J., Li D., Jin J., Wu L. Binding analysis of farrerol to lysozyme by spectroscopic methods // Spectrochim. Acta Part A – 2007. – Vol. 68. – P. 354–359. http://dx.doi.org/10.1016/j.saa.2006.11.045

20. Gowda B., Mallappa M., Gowda J., Rengasamy R. Interaction of ketoconazole with bovine serum albumin: electrochemical, spectroscopic and molecular modeling studies // J. Appl. Pharm. Sci. – 2015. – Vol. 5. – P. 037-044. http://dx.doi.org/ 10.7324/JAPS.2015.58.S6

21. Abu Teir M.M., Ghithan J., Abu-Taha M.I., Darwish S.M., Abu-hadid M.M. Spectroscopic approach of the interaction study of ceftriaxone and human serum albumin // J. Biophys. Struct. Biol. – 2014. – Vol. 6. – P. 1-12. http://dx.doi.org/10.5897/JBSB2013.0045

22. Hamdi O., Feroz S., Shilpi J., Anouar El. H., Mukarram A., Mohamad S.B., Tayyab S., Awang K. Spectrofluorometric and molecular docking studies on the binding of curcumenol and curcumenone to human serum albumin // Int. J. Mol. Sci. – 2015. – Vol. 16. – P. 5180-5193. http://dx.doi.org/10.3390/ijms16035180

23. Salam M.A., Rokonujjaman M., Rahman A., Sultana U.N., Zakir S.M. Study of in Vitro Interaction of Sildenafil Citrate with Bovine Serum Albumin by Fluorescence Spectroscopy // Pharmacology & Pharmacy – 2015. – Vol. 6. – P. 94-101. http://dx.doi.org/10.4236/pp.2015.62012

24. Meti M.D., Nandibewoor S.T., Joshi S.D., More U.A., Chimatadar S.A. Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin // J. Pharm. Anal. –2015. – Vol. 5. – P. 249–255. http://dx.doi.org/10.1016/j.jpha.2015.01.004

25. Naik P.N., Nandibewoor S.T., Chimatadar S.A. Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling // J. Pharm. Anal. – 2015. – Vol. 5. – P. 143–152. http://dx.doi.org/10.1016/j.jpha.2015.01.003

26. Khan S.N., Islam B., Khan A.U. Probing midazolam interaction with human serum albumin and its effect on structural state of protein // Int. J. Integ. Biol. – 2007. – Vol. 1. – P. 102–112.

27. Valeur B., Brochon J.C. New Trends in Fluorescence Spectroscopy 6th edn (Berlin : Springer); 1999, pp. 25–28.

28. Lakowicz J.R. Principles of Fluorescence Spectroscopy 3rd edn New York:Springer; 2006; 954 p.

29. Sahoo B.K., Ghosh K.S., Dasgupta S. Molecular interactions of isoxazolcurcumin with human serum albumin: Spectroscopic and molecular modeling studies // Biopolymers – 2009. – Vol. 91. – P. 108–119. http://dx.doi. org/10.1002/bip.21092

30. Silva D., Cortez C.M., Cunha-Bastos J., Louro S.R.W. Methyl parathion interaction with human and bovine serum albumin // Toxicol. Lett. – 2004. – Vol. 147. – P. 53–61. http://dx.doi.org/10.1016/j.toxlet.2003.10.014

31. Ross P.D., Subramanian S. Thermodynamics of protein association reactions: Forces contributing to stability // Biochemistry. – 1981. – Vol. 20. – P. 3096–3102. http://dx.doi.org/10.1021/bi00514a017

32. Aki H., Yamamoto M. Thermodynamics of the binding of phenothiazines to human plasma, human serum albumin and alpha 1-acid glycoprotein: a calorimetric study // J. Pharm. Pharmacol. – 1989. – Vol. 41. – P. 674-679. http://dx.doi.org/10.1111/j.2042-7158.1989.tb06339.x

33. Miller J.N. Recent advances in molecular luminescence analysis // Proc. Anal. Div. Chem. Soc. – 1979. – Vol. 16, No 7. – Р. 203–208.

34. Wu P., Brand L. Resonance energy transfer: Methods and applications // Anal. Biochem. – 1994. – Vol. 218. – P. 1–13.

35. Forster T. Zwischenmolekulare energiewanderung und fluoreszenz // Ann. Phys. – 1948. – Vol. 2. – P. 55–75.

36. Xiao J.B., Shi J., Cao H., Wu S.D., Ren F.L., Xu, M. Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method // J. Pharm. Biomed. Anal. – 2007. – Vol. 45. – P. 609–615. http://dx.doi.org/10.1016/j.jpba.2007.08.032





DOI: https://doi.org/10.18524/2304-0947.2017.4(64).115917

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