Optimization on fc for improvement of stability and aggregation resistance
文献类型：期刊论文
| 作者 | Chen, Xiaobo1,2; Zeng, Fang1,2; Huang, Tao3; Cheng, Liang3; Liu, Huan1; Gong, Rui1 |
| 刊名 | Current pharmaceutical biotechnology
 |
| 出版日期 | 2016 |
| 卷号 | 17期号:15页码:1353-1359 |
| 关键词 | Fc Monoclonal antibody Fc-fusion protein Stability Aggregation |
| ISSN号 | 1389-2010 |
| DOI | 10.2174/1389201017666161117145312 |
| 通讯作者 | Liu, huan(liuhuan@wh.iov.cn) ; Gong, rui(gongr@wh.iov.cn) |
| 英文摘要 | Fc-based therapeutics including therapeutic full-size monoclonal antibodies (mabs) and fcfusion proteins represent fastest-growing market in biopharmaceutical industrial. however, one major challenge during development of fc-based therapeutics is how to maintain their efficacy in clinic use. many factors may lead to failure in final marketing. for example, the stability and aggregation resistance might not be high enough for bearing the disadvantages during fermentation, purification, formulation, storage, shipment and other steps in manufacture and sale. low stability and high aggregation tendency lead to decreased bioactivity and increased risk of immunogenicity resulting in serious side effect. because fc is one of the major parts in monoclonal antibodies and fc-fusion proteins, engineering of fc to increase its stability and reduce or eliminate aggregation due to incorrect association are of great importance and could further extend the potential of fc-based therapeutics. lots of studies focus on fc optimization for better physical and chemical characteristics and function by structured-based computer-aid rational design, high-throughput screening expression system selection and other methods. the identification of optimized fc mutants increases the clinic potential of currently existed therapeutics mabs and fc-fusion proteins, and accelerates the development of new fc-based therapeutics. here we provide an overview of the related field, and discuss recent advances and future directions in optimization of fc-based therapeutics with modified stability and aggregation resistance. |
| WOS关键词 | JAPANESE ENCEPHALITIS-VIRUS ; YEAST SURFACE DISPLAY ; ANTIBODY DOMAIN C(H)3 ; MONOCLONAL-ANTIBODY ; PROTEIN AGGREGATION ; DIRECTED EVOLUTION ; PRONE REGIONS ; THERAPEUTIC PROTEINS ; CONSTANT DOMAINS ; RECEPTOR |
| WOS研究方向 | Biochemistry & Molecular Biology ; Pharmacology & Pharmacy |
| WOS类目 | Biochemistry & Molecular Biology ; Pharmacology & Pharmacy |
| 语种 | 英语 |
| WOS记录号 | WOS:000390351700007 |
| 出版者 | BENTHAM SCIENCE PUBL LTD |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2373483 |
| 专题 | 武汉病毒研究所 |
| 通讯作者 | Liu, Huan; Gong, Rui |
| 作者单位 | 1.Chinese Acad Sci, Wuhan Inst Virol, CAS Key Lab Emerging Pathogens & Infect, 44 Xiao Hong Shan, Wuhan 430071, Hubei, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Novo Nordisk Res Ctr China, Discovery Screening Dept, Beijing 102206, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chen, Xiaobo,Zeng, Fang,Huang, Tao,et al. Optimization on fc for improvement of stability and aggregation resistance[J]. Current pharmaceutical biotechnology,2016,17(15):1353-1359. |
| APA | Chen, Xiaobo,Zeng, Fang,Huang, Tao,Cheng, Liang,Liu, Huan,&Gong, Rui.(2016).Optimization on fc for improvement of stability and aggregation resistance.Current pharmaceutical biotechnology,17(15),1353-1359. |
| MLA | Chen, Xiaobo,et al."Optimization on fc for improvement of stability and aggregation resistance".Current pharmaceutical biotechnology 17.15(2016):1353-1359. |
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来源：武汉病毒研究所
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