IgG-Fc融合蛋白的研究进展  

Advances in research on Ig G-Fc fusion proteins

作　　者：陈沁韵 万延民[1] 张晓燕[1,2] 

机构地区：[1]上海市公共卫生临床中心,上海201508 [2]复旦大学生物医学研究院,上海200032

出　　处：《中国生物制品学杂志》2015年第11期1223-1227,共5页Chinese Journal of Biologicals

基　　金：国家重点基础研究发展计划(973)(CB542500)

摘　　要：IgG-Fc融合蛋白是将生物活性蛋白与IgG的铰链区和Fc片段进行基因重组而表达的融合蛋白。IgG-Fc融合蛋白不仅可发挥所融合蛋白的生物学活性,还赋予其类似抗体的特性,包括延长血浆半衰期以及Fc片段特有的一系列效应功能,并已广泛应用于临床治疗、生物医学研究等领域。合理优化IgG-Fc融合蛋白是未来发展趋势,选择合适的IgG亚类作为融合载体,采用Fc片段单个或多个氨基酸序列修饰、糖基化改造等,提高融合蛋白的血浆半衰期、优化融合蛋白的效应功能,最终达到最佳免疫治疗效果。本文对IgG-Fc融合蛋白的功能、相应优化策略作一综述,并介绍了其临床研究现状。Ig G-Fc fusion proteins are molecules in which biologically active proteins are fused genetically to the hinge region and Fc fragment of immunoglobulin G.Ig G-Fc fusion proteins can exert biological functions of fused peptides or proteins and endow Ig G-like properties including long plasma half-life and additional Fc fragment properties,which have been widely used for clinical therapy,biomedical research and other fields.Reasonable optimization of Ig G-Fc fusion proteins is a trend in future.Selection of appropriate Ig G subclasses as carriers as well as modification of amino acid sequences and glycosylation of Fc fragment can prolong the plasma half-life and optimize the effector function of fusion protein so as to obtain an ideal immunotherapeutic effect.This paper summarizes the function and optimization strategy of Ig G-Fc fusion proteins and introduce their current status in clinical research.

关 键 词：IgG-Fc 融合蛋白 

分 类 号：Q511[生物学—生物化学] Q819