期刊
FRONTIERS IN IMMUNOLOGY
卷 8, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fimmu.2017.01860
关键词
monoclonal antibody; Fc-fusion protein; Fc-based therapeutics; optimization; physicochemical property; stability; aggregation
类别
资金
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDA12020346]
- Key Program of Chinese Academy of Sciences [ZDRW-ZS-2016-4]
- National Key Research and Development Program of China [2016YFC1202902]
- One-Three-Five Strategic Programs of Wuhan Institute of Virology, Chinese Academy of Sciences [Y605221SA1]
- Wuhan Key Laboratory on Emerging Infectious Diseases and Biosafety
Therapeutic monoclonal antibodies and Fc-fusion proteins are successfully used in treatment of various diseases mainly including cancer, immune disease, and viral infection, which belong to the Fc-based therapeutics. In recent years, engineered Fc-derived antibody domains have also shown potential for Fc-based therapeutics. To increase the druggability of Fc-based therapeutic candidates, many efforts have been made in optimizing physicochemical properties and functions mediated by Fc fragment. The desired result is that we can simultaneously obtain Fc variants with increased physicochemical properties in vitro and capacity of mediating appropriate functions in vivo. However, changes of physicochemical properties of Fc may result in alternation of Fc-mediated functions and vice versa, which leads to undesired outcomes for further development of Fc-based therapeutics. Therefore, whether modified Fc fragments are suitable for achievement of expected clinical results or not needs to be seriously considered. Now, this question comes to be noticed and should be figured out to make better translation from the results of laboratory into clinical applications. In this review, we summarize different strategies on engineering physicochemical properties of Fc, and preliminarily elucidate the relationships between modified Fc in vitro and the subsequent therapeutic influence in vivo.
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