受体
抗体
免疫球蛋白Fc片段
碎片结晶区
化学
免疫球蛋白G
分子生物学
免疫学
细胞生物学
生物
计算生物学
生物化学
作者
G Hale,Jelle De Vos,Alastair Douglas Davy,Koen Sandra,Ian B. Wilkinson
出处
期刊:mAbs
[Informa]
日期:2024-09-15
卷期号:16 (1)
被引量:1
标识
DOI:10.1080/19420862.2024.2402701
摘要
Elimination of the binding of immunoglobulin Fc to Fc gamma receptors is highly desirable for the avoidance of unwanted inflammatory responses to therapeutic antibodies and fusion proteins. Many different approaches have been used in the clinic, but they have not been systematically compared. We have now produced a matched set of anti-CD20 antibodies with different Fc subclasses and variants and compared their activity for binding to C1q, Fc-gamma receptors and in cell-based assays. Most of the variants still have significant levels of activity in one or more of these assays and many of them have impaired temperature stability compared with the corresponding wild-type antibody.
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