Mono-PEGylation of ribonuclease A: High PEGylation efficiency by thiolation with small molecular weight reagent
文献类型：期刊论文
| 作者 | Liu, Shenxiang1,2; Sun, Lijing1; Wang, Jun1; Ma, Guanghui1; Su, Zhiguo1; Hu, Tao1 |
| 刊名 | PROCESS BIOCHEMISTRY
 |
| 出版日期 | 2012-09-01 |
| 卷号 | 47期号:9页码:1364-1370 |
| 关键词 | PEGylation Mono-PEGylation Polyethylene glycol Ribonuclease A Thiolation |
| ISSN号 | 1359-5113 |
| 通讯作者 | Hu, T |
| 英文摘要 | PEGylation can improve the therapeutic potential of ribonuclease A (RNase A), a cancer chemotherapeutic agent. However, the common PEGylation that targets at the e-amino groups of proteins can lead to imprecise control of the stoichiometry of the protein-PEG conjugate (i.e., mono-, di- and multi-PEGylated protein). To prepare a PEGylated therapeutic protein, it is desirable that the protein is mono-PEGylated for industrial production, convenient purification and analytical characterization. Here, N-hydroxysuccinimide esters of S-acetylthioacetic acid (SATA) and 2-iminothiolane (IT) were used to introduce thiol groups on RNase A. followed by maleimide chemistry based PEGylation of the thiolated RNase A. Interestingly, the yield of mono-PEGylated RNase A was higher than 60%, and di- or multi-PEGylated RNase A were absent in the PEGylated product. Presumably, the limited number and low solvent accessibility of the introduced thiol group favored mono-PEGylation of RNase A. As compared to the unmodified RNase A. the mono-PEGylated RNase A showed slightly decreased enzymatic activity, increased anti-proliferative ability and unchanged structural properties. Our study is expected to control the PEGylation process and optimize the industrial pharmaceutical production of PEGylated proteins. (C) 2012 Elsevier Ltd. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Technology |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering, Chemical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering |
| 关键词[WOS] | PROTEIN PEGYLATION ; ETHYLENE-GLYCOL ; PEPTIDE ; THERAPEUTICS ; HEMOGLOBIN ; ENZYMES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000306777400010 |
| 公开日期 | 2013-10-16 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/3550]  |
| 专题 | 过程工程研究所_生化工程国家重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Shenxiang,Sun, Lijing,Wang, Jun,et al. Mono-PEGylation of ribonuclease A: High PEGylation efficiency by thiolation with small molecular weight reagent[J]. PROCESS BIOCHEMISTRY,2012,47(9):1364-1370. |
| APA | Liu, Shenxiang,Sun, Lijing,Wang, Jun,Ma, Guanghui,Su, Zhiguo,&Hu, Tao.(2012).Mono-PEGylation of ribonuclease A: High PEGylation efficiency by thiolation with small molecular weight reagent.PROCESS BIOCHEMISTRY,47(9),1364-1370. |
| MLA | Liu, Shenxiang,et al."Mono-PEGylation of ribonuclease A: High PEGylation efficiency by thiolation with small molecular weight reagent".PROCESS BIOCHEMISTRY 47.9(2012):1364-1370. |
入库方式： OAI收割
来源：过程工程研究所
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