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Разработка и регистрация лекарственных средств

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ДАУНСТРИМ-ПРОЦЕСС ОЧИСТКИ БИОФАРМАЦЕВТИЧЕСКИХ БЕЛКОВ

Аннотация

Развитие биофармацевтической отрасли начинается с разработки эффективных продуцентов. Однако чем сложнее белок и его продуцент, тем большее количество примесей, среди которых эндотоксины, белки хозяина, вирусы, родственные примеси, агрегаты и высокомолекулярные контамитанты, синтезируется или накапливается в ходе процесса получения. Статья описывает под ходы к выделению и очистке биофармацевтических белков (даунстрим-процесс). Обсуждаются основные хроматографические и нехроматографические методы.

Об авторе

Д. А. Гусаров
Научно-производственная биотехнологическая платформа «ЭкспертБИОТЕ»
Россия


Список литературы

1. D. Scott. Biopharmaceutical Manufacturing // Рresentation on Lab Basics for the Biotech Industry, MIP480. 2009.

2. L. Anderson, F. Unger. Synthetic studies on structural elements of the hydrophobic region present in bacterial endotoxins. In Bacterial Lipopolysaccharides // American Chemical Society. ACS Symposium Series. 1983. № 231. P. 1.

3. K.C. Hou, R. Zaniewski. Scaling-up of affinity chromatography by radial-flow cartridges // Biotechnol. Appl. Biochem. 1990. V. 12. P. 315-321.

4. Endotoxins: Pyrogens, LAL Testing and Depyrogenation, 3rd Edition / Ed. by K.L. Williams, M. Dekker // Drugs and Pharmaceutical sciences. 2007. V. 167. 440 p.

5. X. Du, A. Poltorak, Y. Wei. Three novel mammalian toll-like receptors: gene structure, expression and evolution // Eur Cytokine Netw Eur Cytokine Netw. 2000. V. 11. P. 362-371.

6. K. Gerhold, K. Bluemchen, A. Franke, Ph. Stock, E. Hamelmann. Exposure to endotoxin and allergen in early life and its effect on allergen sensitization in mice // J. Allergy Clin. Immunol. 2003. V. 112 (2). P. 389-396.

7. R.A. Nash, A.H. Wachter. Pharmaceutical Process Validation, an international third edition, revised and expanded // Drugs and Pharmaceutical sciences. 2003. V. 129. 536 p.

8. E.T. Rietschel, T. Kirikae, F.U. Schade, U. Mamat, G. Schmidt, H. Loppnow, A.J. Ulmer, U. Zaehringer, U. Seydel, F. Di Padova, M. Schreier, H. Brade. Bacterial endotoxin: molecular relationships of structure to activity and function // FASEB J. 1994. V. 8. P. 217-225.

9. J. Schletter, H. Heine, A.J. Ulmer, E.T. Rietschel. Molecular mechanisms of endotoxin activity // Arch. Microbiol. 1995. V. 164. P. 383-389.

10. L. Li. Protein and endotoxin interactions and endotoxin removal from protein solutions: Diss.. Doctor of Philosophy. - New Jersey Institute of Technology. 1999.

11. C. Galanos, O. Luederitz, E. Rietschel, O. Westphal, H. Brade, L. Brade, M. Freudenberg, U. Schade, M. Imoto, H. Yoshimura, S. Kusumoto, T. Shiba. Synthetic and natural Escherichia coli free lipid A express identical endotoxic activities // Eur. J. BioChem. 1985. V. 148. P. 1-5.

12. M. Helander, B. Lindner, H. Brade, H. Altmann, A. Lindberg, E. Rietschel, U. Zaehringer. Chemical structure of the lipopolysaccharide of Haemophilus influenzae strain I-69 Rd-/b+. Description of a novel deep-rough chemotype / Eur. J. Biochem. 1988. V. 177. P. 483-492.

13. U. Zaehringer, B. Lindner, E. Rietschel. Molecular structures that influence the immunomodulatory properties of the lipid A and inner core region oligosaccharides of bacterial lipopolysaccharides // Adv. Carbohydr. Chem. Biochem. 1994. V. 50. P. 211-276.

14. S.N. Vogel, M.M. Hogan. Role of cytokines in endotoxin-mediated host responses // Immunophysiology: the role of cells and cytokines in immunity and inflammation / Ed. by J.J. Oppenheim, E.M. Shevach. - Oxford: Oxford University Press, 1990. P. 238-252.

15. D. Nogare. Septic shock // Am. J. Med. Sci. 1991. V. 302. P. 50-65.

16. K. Hou, R. Zaniewski. Depyrigenation by endotoxin removal with positively charged depth filter cartridge // J. Parenter. Sci. Technol. 1990. V. 44. P. 204-209.

17. F.B. Anspach. Removal of endotoxins by affinity sorbents // J. Biochem. Biophys. Methods. 2001. V. 49. P. 665-681.

18. J. Shands, J. Graham, K. Nath. The morphologic structure of isolated bacterial lipopolysaccharide // J. Mol. Biol. 1967. V. 25. P. 15-16.

19. E. Hannekart-Pokorni, D. Dekagel, F. Depuydt. Macromolecular structure of lipopolysaccharides from gram-negative bacteria // Eur. J. Biochem. 1973. V. 38. P. 6-13.

20. U. Seydel, H. Labischinski, M. Kastowsky. Conformations of endotoxin and their relationship to biological activity // Immunobiology. 1993. V. 187. P. 191-197.

21. M. Kastowski, T. Gutberlet, H. Bradaczek. Molecular modeling of the three-dimensional structure and conformational flexibility of bacterial lipopolysaccharide // J. Bacteriol. 1992. V. 174. P. 4798-4806.

22. D. Petsch, F. Anspach. Endotoxin removal from protein solutions // J. Biotechnol. 2000. V. 76. P. 97-119.

23. L. Li, R. Luo. Protein concentration effect on proteinlipopolysaccharide (LPS) binding and endotoxin removal // Biotechnol. Lett. 1997. V. 19 (2). P. 135-138.

24. L. Li, R. Luo. Protein and endotoxin interactions and endotoxin removal from protein solutions // Separation Sciences and Technology. 1999. V. 34(9). P. 1729-1741.

25. L. Li. Luo RG: Use of Calcium to re-aggregate lipopolysaccharide (LPS) in hemoglobin solutions and the subsequent removal of endotoxin by ultra filtration // Biotechnol. Tech. 1998. V. 12(2). P. 119-122.

26. D. Morrison, L. Leive. Fractions of lipopolysaccharide from Escherichia coli O111:B4 prepared by two extraction procedures // J. Biol. Chem. 1975. V. 250. P. 2911-2919.

27. T.E. Karplus, R.J. Ulevitch, C.B. Wilson. A new method for reduction of endotoxin contaminations from protein solutions // J. Immunol. Methods. 1987. V. 105. P. 211-220.

28. Y. Aida, M. Pabst. Removal of endotoxin from protein solutions by phase separation using Triton X-114 // J. Immunol. Methods. 1990. V. 132. P. 191-195.

29. M.J. Wilson, C.L. Haggart, S.P. Gallagher, D. Walsh. Removal of tightly bound endotoxin from biological products // J. Biotechnol. 2001. V. 88. P. 67-75.

30. R. Bischoff, D. Speck, P. Lepage, L. Delatre, K. Leoux, S. Brown. Roitsch C: Purification and biochemical characterization of recombinant 1-antitrypsin variants expressed in Escherichia coli // Biochemistry. 1991. V. 30. P. 3464-3472.

31. D. Petsch, E. Rantze, F. Anspach. Selective adsorption of endotoxin inside a polycationic network of flatsheet microfiltration membranes // J. Mol. Recognit. 1998. V. 11. P. 222-231.

32. S.-H. Pyo, H.-B. Park, S.-S. Hong, J.-H. Kim. A largescale purification of paclitaxel from cell cultures of Taxus chinensis // Biotechnol. Lett. 2001. V. 23. P. 737-740.

33. P. Reichelt, C. Schwartz, M. Donzeau. Single step protocol to purify recombinant proteins with low endotoxin contents // Prot. Exp. Purif. 2006. V. 46. P. 483-488.

34. R.H. Chen, C-J. Huang, B.S. Newton, G. Ritter, L.J. Old, C.A. Batt. Factors affecting endotoxin removal from recombinant therapeutic proteins by anion exchange chromatography // Prot. Exp. Purif. 2009. V. 64. P. 76-81.

35. J.P. Nolan, J.J. McDevitt, G.S. Goldmann. Physiochemical properties of quartz controlling biological activity. Silica, Silicosis and Cancer-Surface Properties // Proc. Soc. Exp. Biol. Med. 1975. V. 149. P. 766-771.

36. M. Nagaki, R. Hughes, J. Lau, R. Williams. Removal of endotoxin and cytokines by adsorbents and the effect of plasma protein binding // Int. J. Artif. Organs. 1991. V. 14. P. 43-50.

37. Y. Yasaka, M. Tanaka. The distribution of the blood flow during exercise in chronic heart failure - compensatory mechanism to the decreased cardiac output // J. Chromatogr. B. 1994. V. 659. P. 139-143.

38. Y. Li, R. Lander, W. Manger, A. Lee. Determination of lipid profile in meningococcal polysaccharide using reversed-phase liquid chromatography // J. Chromatogr. B. 2004. V. 804. P. 353-358.

39. K.M. Gooding, F.E. Regnier. HPLC of Biological Macromolecules. Methods and Applications. - N.Y. 1990. 796 p.

40. E.P. Kroeff, R.A. Owens, E.L. Campbell, R.D. Johnson, H.I. Marks. Production scale purification of biosynthetic human insulin by reversed-phase high-performance liquid chromatography // J. Chromatogr. 1989. V. 461. P. 45-61.

41. Д.А. Гусаров, В.В. Востриков, Е.А. Ручко, В.А. Ласман, А.В. Михалев, Д.И. Баирамашвили. Способы очистки биофармацевтических белков от эндотоксинов клеточной стенки / Биотехнология. 2006. № 2. С. 44-49.

42. G. Karlsson, P. Gellerfors, A. Persson, B. Noren, P. Edlund, C. Sandberg, S. BirnBaum. Separation of oxidized and deamidated human growth hormone variants by isocratic reversed-phase high-performance liquid chromatography // J. Chromatogr. A. 1999. V. 855. P. 147-155.

43. S. Sainathan, L. Tu, K. Bishnupuri, M. Han, A. Li, R. Newberry, K. McDonald, D. Crimmins, C. Houchen, S. Anant, B. Dieckgraefe. PEGylated murine granulocyte-macrophage colony-stimulating factor: production, purification, and characterization // Prot. Exp. Purif. 2005. V. 44. P. 94-103.

44. S. Hershenson, Z. Shaked. Purification of recombinant beta-interferon incorporating RP-HPLC, United States Patent. 1990. № 4, 894, 330.

45. Endotoxin Removal from Proteins. URL: http:/www. proteinchemist.com/tutorial/endotoxin.html (дата обращения 28.07.2016).

46. R. Shimp, jr., L. Martin, Y. Zhang, B. Henderson, P. Duggan, N. MacDonald, J. Lebowitz, A. Saul, D. Narum. Identification and Characterization of the Plasmodium yoelii PyP140/RON4 Protein, an Orthologue of Toxoplasma gondii RON4, Whose Cysteine-Rich Domain Does Not Protect against Lethal Parasite Challenge Infection // Prot. Exp. Purif. 2006. V. 50. P. 58-67.

47. Merck-USA. Removal of pyrogens and yeast proteins from hepatitis B virus surface antigen, United States Patent. 1989. № 4,707,542.

48. J. Lopes, W. Inniss. Electron Microscopy of Effect of Polymyxin on Escherichia coliLipopolysaccharide // J. Bacteriol. 1969. V. 100. P. 1128-1130.

49. A. Horenstein, F. Crivellin, A. Funaro, M. Said, F. Malavasi. Human CD38: a glycoprotein in search of a function // J. Immunol. Methods. 2003. V. 275. P. 99-112.

50. K. Hou, R. Zaniewski. Endotoxin removal by anionexchange polymeric matrix // Biotechnol. Bioeng. 1990. V. 12. P. 315-324.

51. F. Anspach, O. Kilbeck. Removal of endotoxins by affinity sorbents // J. Chromatogr. A. 1995. V. 711. P. 81-87.

52. B.A. Newton. The properties and mode of action of the polymyxins // Bac. Rev. 1956. V. 20. P. 14-27.

53. C. Damais, C. Jupin, M. Parant, L. Chedid. Induction of human interleukin-1 production by polymyxin B // J. Immunol. Methods. 1987. V. 101. P. 51-56.

54. S. Minobe, T. Sato, T. Tosa, I. Chibata. Characteristics of immobilized histamine for pyrogen adsorption // J. Chromatogr. 1983. V. 262. P. 193-197.

55. S. Minobe, T. Watanabe, T. Sato, T. Tosa. Charactristics and applications of adsorbents for pyrogen removal // Biotechnol. Appl. Biochem. 1988. V. 10. P. 143-148.

56. H. Choi, R. Yang, M. Kunioka. Surface modification of polyhydroxyalkanoate films and their interaction with human fibrablasts // J. Appl. Polym. Sci. 1995. V. 58. P. 807-811.

57. M. Sakata, M. Todokoro, C. Hirayama. Removal of endotoxin from protein solution using poly(ε-lysine)- immobilized cellulose beads // Am. Biotechnol. Lab. 2002. V. 20. P. 36-41.

58. G. Carta, A. Jungbauer. Protein Chromatography: Process Development and Scale-Up // WILEY-VCH Verlag GmbH & Co. - Weinheim. 2010.

59. D. Voet, J. Voet. Biochemistry. - New York: John Wiley and Sons, 1990.

60. G. Subramanian. Bioseparation and bioprocessing. A handbook // WILEY-VCH Verlag GmbH & Co. - Weinheim. 2007.

61. Y. Li, O. Galperina. PDA Viral Safety Workshop. - Germany. 2005.

62. J. Poreth, P. Flodin. Gel Filtration: A Method for Desalting and Group Separation // Nature. 1983. V. 2. P. 1657-1659.

63. Патент РФ № 2187363. Способ получения гидрофильного геля / А.В. Смирнов, Е.А. Гукасова, Д.И. Баирамашвили, А.И. Мирошников. 2002.

64. Endotoxin Removal from Proteins. URL: http:/www. proteinchemist.com/tutorial/endotoxin.html (дата обращения 28.07.2016).

65. R. Shimp-jr., L. Martin, Y. Zhang, B. Henderson, P. Duggan, N. MacDonald, J. Lebowitz, A. Saul, D. Narum. Identification and Characterization of the Plasmodium yoelii PyP140/RON4 Protein, an Orthologue of Toxoplasma gondii RON4, Whose Cysteine-Rich Domain Does Not Protect against Lethal Parasite Challenge Infection // Prot. Exp. Purif. 2006. V. 50. P. 58-67.

66. Merck-USA. Removal of pyrogens and yeast proteins from hepatitis B virus surface antigen, United States Patent. 1989. № 4,707,542.

67. J. Lopes, W. Inniss. Electron Microscopy of Effect of Polymyxin on Escherichia coliLipopolysaccharide // J. Bacteriol. 1969. V. 100. P. 1128-1130.

68. A. Horenstein, F. Crivellin, A. Funaro, M. Said, F. Malavasi. Human CD38: a glycoprotein in search of a function // J. Immunol. Methods. 2003. V. 275. P. 99-112.

69. K. Hou, R. Zaniewski. Endotoxin removal by anionexchange polymeric matrix // Biotechnol. Bioeng. 1990. V. 12. P. 315-324.

70. F. Anspach, O. Kilbeck. Removal of endotoxins by affinity sorbents // J. Chromatogr. A. 1995. V. 711. P. 81-87.

71. B.A. Newton. The properties and mode of action of the polymyxins // Bac. Rev. 1956. V. 20. P. 14-27.

72. C. Damais, C. Jupin, M. Parant, L. Chedid. Induction of human interleukin-1 production by polymyxin B // J. Immunol. Methods. 1987. V. 101. P. 51-56.

73. S. Minobe, T. Sato, T. Tosa, I. Chibata. Characteristics of immobilized histamine for pyrogen adsorption // J. Chromatogr. 1983. V. 262. P. 193-197.

74. S. Minobe, T. Watanabe, T. Sato, T. Tosa. Charactristics and applications of adsorbents for pyrogen removal // Biotechnol. Appl. Biochem. 1988. V. 10. P. 143-148.

75. H. Choi, R. Yang, M. Kunioka. Surface modification of polyhydroxyalkanoate films and their interaction with human fibrablasts // J. Appl. Polym. Sci. 1995. V. 58. P. 807-811.

76. M. Sakata, M. Todokoro, C. Hirayama. Removal of endotoxin from protein solution using poly(ε-lysine)- immobilized cellulose beads // Am. Biotechnol. Lab. 2002. V. 20. P. 36-41.


Рецензия

Для цитирования:


Гусаров Д.А. ДАУНСТРИМ-ПРОЦЕСС ОЧИСТКИ БИОФАРМАЦЕВТИЧЕСКИХ БЕЛКОВ. Разработка и регистрация лекарственных средств. 2016;(3):88-99.

For citation:


Gusarov D.A. DOWNSTREAM PROCESS OF BIOPHARMACEUTICALS. Drug development & registration. 2016;(3):88-99. (In Russ.)

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