| PEGylation of rhIL-1RA increased its solution stability at room temperature | |
| Yu, Pengzhan1,2; Qin, Dan2; Qin, Guohong1,2; Fan, Bei1; Ma, Guanghui1; Su, Zhiguo1; Su, ZG | |
| 2009-12-01 | |
| Source Publication | PROCESS BIOCHEMISTRY
 |
| ISSN | 1359-5113 |
| Volume | 44Issue:12Pages:1340-1345 |
| Abstract | Recombinant human interleukin-1 receptor antagonist (rhIL-1RA) is an important cytokine in the treatment of inflammatory diseases. However, it is instable in aqueous solution and prone to degrade without the addition of any excipient. Following the 30- or 60-day storage in 50 mM sodium acetate (pH 5.0) at room temperature, rhIL-1RA markedly degraded into three species (denoted as P1, P2 and P3 in this study), the bioactivities of which to a different extent was lost (from 9.72 x 104 Ul/mg to 3.07 x 10(3) Ul/mg for P1, 5.49 x 10(3) Ul/mg for P2, 1.09 X 10(4) Ul/mg for P3, respectively). To solve this problem, we prepared the mono-PEGylated rhIL-IRA with propionaldehyde mPEG (ALD-PEG, M(w) 5000 Da). The conjugate showed more favorable stability than original protein, and remained homogeneous under the similar storage conditions. In addition, the activity of the conjugate was well retained (from 5.80 x 10(4) Ul/mg to 4.92 X 10(4) Ul/mg), compared to that of original protein. The results based on the combination analysis of CD, ion exchange chromatography and RP-HPLC, revealed that the stability improvement of rhIL-1RA majorly benefited from the PEG strands protection against the protein conformational changes occurred during the storage. (C) 2009 Published by Elsevier Ltd. |
| Keyword | Recombinant Human Interleukin-1 Receptor Antagonist Pegylation Aqueous Stability Conformational Changes Chromatography |
| Subtype | Article |
| WOS Headings | Science & Technology ; Life Sciences & Biomedicine ; Technology |
| DOI | 10.1016/j.procbio.2009.07.010 |
| Indexed By | SCI |
| Language | 英语 |
| WOS Keyword | INTERLEUKIN-1 RECEPTOR ANTAGONIST ; AGGREGATION ; FORMULATION ; IL-1 ; THERMOSTABILITY ; KINETICS ; BINDING ; GROWTH ; ASSAY |
| WOS Research Area | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering |
| WOS Subject | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering, Chemical |
| WOS ID | WOS:000272071900006 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Version | 出版稿 |
| Identifier | http://ir.ipe.ac.cn/handle/122111/6539 |
| Collection | 生化工程国家重点实验室 |
| Corresponding Author | Su, ZG |
| Affiliation | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100080, Peoples R China 2.Jiangsu Simcere Pharmaceut R&D Co Ltd, Beijing 100007, Peoples R China |
| Recommended Citation GB/T 7714 | Yu, Pengzhan,Qin, Dan,Qin, Guohong,et al. PEGylation of rhIL-1RA increased its solution stability at room temperature[J]. PROCESS BIOCHEMISTRY,2009,44(12):1340-1345. |
| APA | Yu, Pengzhan.,Qin, Dan.,Qin, Guohong.,Fan, Bei.,Ma, Guanghui.,...&Su, ZG.(2009).PEGylation of rhIL-1RA increased its solution stability at room temperature.PROCESS BIOCHEMISTRY,44(12),1340-1345. |
| MLA | Yu, Pengzhan,et al."PEGylation of rhIL-1RA increased its solution stability at room temperature".PROCESS BIOCHEMISTRY 44.12(2009):1340-1345. |
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| 20131129-16-复件 1-s2.（579KB） | 限制开放 | CC BY-NC-SA | Application Full Text | |||
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