d(GC) - Association of Biotechnology and Pharmacy

More documents

Recommendations

Info

Current Trends in Biotechnology and Pharmacy Vol. 6 (2) 222-228 April 2012, ISSN 0973-8916 (Print), 2230-7303 (Online) 11. Athmaram, T.N., Saraswat, S., Santhosh, S.R., Singh, A.K., Suryanarayana, W.S., Priya, R., Gopalan, N., Parida, M., Rao, P.V. and Vijayaraghavan, R. (2011). Yeast expressed recombinant Hemagglutinin protein of novel H1N1 elicits neutralising antibodies in rabbits and mice. Virol J. 8: 524. 12. Biesova, Z., Miller, M.A., Schneerson, R., Shiloach, J., Green, K.Y., Robbins, J.B. and Keith, J.M. (2009). Preparation, characterization, and immunogenicity in mice of a recombinant influenza H5 hemagglutinin vaccine against the avian H5N1 A/Vietnam/1203/2004 influenza virus. Vaccine. 27: 6234-6238. 13. Aguilar-Yanez, J.M., Portillo-Lara, R., Mendoza-Ochoa, G.I., Garcia-Echauri, S.A., Lopez-Pacheco, F., Bulnes-Abundis, D., Salgado-Gallegos, J., Lara-Mayorga, I.M., Webb-Vargas Y., Leon-Angel, F.O., Rivero-Aranda, R.E., Oropeza-Almazan, Y., Ruiz-Palacios, G.M., Zertuche-Guerra, M.I., DuBois, R.M., White, S.W., Schultz-Cherry, S., Russell, C.J. and Alvarez, M.M. (2010). An influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli. PLoS One. 5: e11694. 14. Louisirirotchanakul, S., Lerdsamran, H., Wiriyarat, W., Sangsiriwut, K., Chaichoune, K., Pooruk, P., Songserm, T., Kitphati, R., Sawanpanyalert, P., Komoltri, C., Auewarakul, P. and Puthavathana, P. (2007). Erythrocyte binding preference of avian influenza H5N1 viruses. J Clin Microbiol. 45: 2284-2286. Cloning, Expression and purification of H5N1 in E. coli 228 15. Robinson, H.L., Hunt, L.A. and Webster, R.G. (1993). Protection against a lethal influenza virus challenge by immunization with a haemagglutinin-expressing plasmid DNA. Vaccine. 11: 957-960. 16. Webster, R.G., Fynan, E.F., Santoro, J.C. and Robinson, H. (1994). Protection of ferrets against influenza challenge with a DNA vaccine to the haemagglutinin. Vaccine. 12: 1495-1498. 17. Johansson, B.E. (1999). Immunization with influenza A virus hemagglutinin and neuraminidase produced in recombinant baculovirus results in a balanced and broadened immune response superior to conventional vaccine. Vaccine. 17: 2073- 2080. 18. Kodihalli, S., Haynes, J.R., Robinson, H.L. and Webster, R.G. (1997). Cross-protection among lethal H5N2 influenza viruses induced by DNA vaccine to the hemagglutinin. J Virol. 71: 3391-3396. 19. Kodihalli, S., Goto, H., Kobasa, D.L., Krauss, S., Kawaoka, Y. and Webster, R.G. (1999). DNA vaccine encoding hemagglutinin provides protective immunity against H5N1 influenza virus infection in mice. J Virol. 73: 2094-2098. 20. Fang, F., Cai, X.Q., Chang, H.Y., Wang, H.D., Yang, Z.D. and Chen, Z. (2008). Protection abilities of influenza B virus DNA vaccines expressing hemagglutinin, neuraminidase, or both in mice. Acta Virol. 52: 107-112.
Current Trends in Biotechnology and Pharmacy Vol. 6 (2) 229-240 April 2012, ISSN 0973-8916 (Print), 2230-7303 (Online) Chemical Modification of Recombinant Human Interferon Beta-1a Using Linear and Branched mPEGs Ahmad Abolhasani 1 , Sameereh Hashemi-Najafabadi 1* , Mahvash Khodabandeh Shahraki *2 and Zohreh-Azita Sadigh 3 1 Biotechnology Group, Department of Chemical Engineering, Tarbiat Modares University, P. O. Box: 14115/114, Tehran, I. R. Iran 2 National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, I. R. Iran 3 Razi Vaccine and Serum Research Institute, Tehran, I. R. Iran * For correspondence - s.hashemi@modares.ac.ir Abstract Interferon-beta-1a (IFN-β-1a) is used clinically in the treatment of multiple sclerosis. Similar to other biological molecules, IFN-β-1a has a relatively short serum half-life and is rapidly detected by the host’s immune system. PEGylation is a common approach to increase the blood circulation time of therapeutic proteins. In the present study, IFN-β-1a was PEGylated using linear methoxy polyethylene glycols (mPEGs) with molecular weights of 5 and 20 kDa and also 40 kDa branched mPEG-SPA. Prior to PEGylation, the mPEGs were activated by succinimidyl propionic acid (SPA). PEGylation was evaluated by size-exclusion HPLC (SE- HPLC) and Ninhydrin method. In the designed experiments, the factors of mPEG molecular weight, pH, and the molecular ratio of protein to mPEG fractions were studied. The results were analyzed using Design-Expert statistical software and the significant factors were determined. Then, in order to find the optimum conditions, Taguchi method (L 9 array) was used by considering the significant factors. Consequently, the optimum conditions for PEGylation, using 20 kDa linear mPEG-SPA was found to be at pH 8 and the protein to mPEG molar ratio of 1/40. The extents of protein modification were obtained 45.5% and 46.8% by HPLC and Ninhydrin methods, respectively. Optimum PEGylation with 40 kDa branched mPEG-SPA was obtained at pH 8 and protein/mPEG of 1/40. In this case, the Interferon Beta-1a PEGylation 229 extents of protein modification were obtained 46.5% and 47.7% by HPLC and Ninhydrin methods, respectively. The biological activity test showed that the PEGylated protein retained about 80% of its activity, were compared to that of the unmodified protein. Key words: Beta interferon, Biological activity, mPEG-SPA, PEGylation, Taguchi method. Introduction Interferons (IFNs) are a family of cytokines that mediate antiviral, antiproliferative and immunomodulatory effects in response to biological and chemical stimuli. Two types of IFNs are recognized based on their physical and biological properties; type I which contains IFNsα, -β, -κ, -τ, and -ω, and type II the only member of which is IFN-γ (1-5). Recombinant forms of IFN-β-1a (Avonex, Biogen Idec, Rebif and Serono) and IFN-β-1b (Betaferon, Schering AG) have been approved for the treatment of multiple sclerosis (MS), while non-recombinant forms of IFN-β (e.g., Feron and Toray) have been approved in Japan for the treatment of chronic viral hepatitis C (HCV). Therapeutic proteins have poor pharmacokinetic profiles because of their rapid clearance from blood circulation. Polyethylene glycol (PEG) attachment to the proteins offers a solution to these problems. The antiviral and immunomodulator drug, IFN-β-1a, is a common example (6).
Page 3 and 4:
Current Trends in Biotechnology and
Page 5 and 6:
Page 7 and 8:
Page 9 and 10:
Page 11 and 12:
Page 13 and 14:
Page 15 and 16:
Page 17 and 18:
Page 19 and 20:
Page 21 and 22:
Page 23 and 24:
Page 25 and 26:
Page 27 and 28:
Page 29 and 30:
Page 31 and 32:
Page 33 and 34:
Page 35 and 36:
Page 37 and 38:
Page 39 and 40:
Page 41 and 42:
Page 43 and 44:
Page 45 and 46:
Page 47 and 48:
Page 49 and 50:
Page 51 and 52:
Page 53 and 54:
Page 55 and 56:
Page 57 and 58:
Page 59 and 60:
Page 61 and 62:
Page 63 and 64:
Page 65 and 66: Current Trends in Biotechnology and
Page 115: Current Trends in Biotechnology and
Page 147 and 148: 6th Annual Convention of Associatio
show all

d(GC) - Association of Biotechnology and Pharmacy

Create successful ePaper yourself

Delete template?

Save as template?