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Evaluation of physicochemical and stability properties of human growth hormone upon enzymatic PEGylation

Bahman Khameneh, Mohammad Reza Saberi, Mohammad Hassanzadeh-Khayyat, Hamid Mohammadpanah, Morteza Ghandadi, Mehrdad Iranshahi, Ali Baratian, Mahmoud Reza Jaafari

. 2016 ; 14 (4) : 257-264.

Jazyk angličtina Země Česko

Typ dokumentu práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc17012152

Background PEGylation is an increasingly important strategy for improving stability, pharmacokinetic and pharmacodynamic properties of proteins. Objective In this study, site-specific PEGylated human growth hormone (hGH) was prepared by microbial transglutaminase and physicochemical and stability properties of bioconjugates were tested. Method hGH was PEGylated by 20 kDa mPEG-NH2. PEG-hGH was purified by size exclusion chromatography method and analyzed by SDS-PAGE, IEF gel and CD spectroscopy methods. Physicochemical properties, size and zeta potentials, of native and PEGylated hGH were evaluated by Dynamic Light Scattering (DLS) method. Physical and chemical stabilities were assayed at different temperatures (37, 25 and 4 °C) within three weeks by SEC- and RP-HPLC methods, respectively. Results By this preparation method, mono-PEG-hGH was obtained and the secondary structure was unchanged. The DLS results indicated that by PEGylation the size and zeta potentials of the protein were increased and decreased, respectively. These data indicated that PEG chain covered the protein surface. The isoelectric point (pI) of protein was not altered following PEGylation. The results of stability indicated that, the mono-PEG-hGH was considerably more stable especially in elevated temperatures as compared with the non-PEGylated one. Conclusion PEGylation changed the physicochemical properties of hGH and also enhanced the stability of the protein.

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Literatura

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$a Background PEGylation is an increasingly important strategy for improving stability, pharmacokinetic and pharmacodynamic properties of proteins. Objective In this study, site-specific PEGylated human growth hormone (hGH) was prepared by microbial transglutaminase and physicochemical and stability properties of bioconjugates were tested. Method hGH was PEGylated by 20 kDa mPEG-NH2. PEG-hGH was purified by size exclusion chromatography method and analyzed by SDS-PAGE, IEF gel and CD spectroscopy methods. Physicochemical properties, size and zeta potentials, of native and PEGylated hGH were evaluated by Dynamic Light Scattering (DLS) method. Physical and chemical stabilities were assayed at different temperatures (37, 25 and 4 °C) within three weeks by SEC- and RP-HPLC methods, respectively. Results By this preparation method, mono-PEG-hGH was obtained and the secondary structure was unchanged. The DLS results indicated that by PEGylation the size and zeta potentials of the protein were increased and decreased, respectively. These data indicated that PEG chain covered the protein surface. The isoelectric point (pI) of protein was not altered following PEGylation. The results of stability indicated that, the mono-PEG-hGH was considerably more stable especially in elevated temperatures as compared with the non-PEGylated one. Conclusion PEGylation changed the physicochemical properties of hGH and also enhanced the stability of the protein.
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$a Hassanzadeh-Khayyat, Mohammad $u Pharmaceutical Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
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$a Iranshahi, Mehrdad $u Biotechnology Research Center, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
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$a Baratian, Ali $u Department of Pharmaceutics, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
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