期刊
JOURNAL OF APPLIED GLYCOSCIENCE
卷 68, 期 1, 页码 1-9出版社
JAPANESE SOC APPLIED GLYCOSCIENCE
DOI: 10.5458/jag.jag.JAG-2020_0013
关键词
immunoglobulin G; endo-beta-N-acetylglucosaminidase; transglycosylation; remodeling; glycoengineering
The structure of glycans in glycoproteins directly affects their biological aspects, such as binding affinity. Recent progress in glycan remodeling and glycoengineering techniques has led to the development and production of biopharmaceutical glycan-modified antibodies with well-defined and homogeneous glycoforms.
Most functional biopharmaceuticals such as antibodies are glycoproteins carrying N-linked oligosaccharides (N-glycans). In animal cells, these glycans are generally expressed as heterogeneous glycoforms that are difficult to separate into a pure form. The structure of these glycans directly affects several biological aspects of the glycoproteins, especially binding affinity. Therefore, the preparation of glycoproteins with well-defined and homogeneous glycoforms is necessary for functional studies and improved efficacy, particularly for biopharmaceuticals. This review describes the recent remarkable progress in the development and production of biopharmaceutical glycan-modified antibodies, through the use of glycan remodeling using microbial endoglycosidases and sophisticated glycoengineering techniques utilizing microbial enzymatic reaction mechanisms.
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