Introduction to Therapeutic Antibodies

R. R. Nair
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Abstract

Antibodies are immunoglobulins that are part of the humoral immune response and are secreted by the B-cells (plasma cells). Antibodies act by binding to either soluble antigens or ligands that are expressed on the surface of organisms or cells. In terms of structure, antibodies are Y-shaped glycoproteins made up of two heavy chain polypeptides and two light chain polypeptides that are held together by disulfide bridges. The light and the heavy chain are made up of constant regions and variable regions with light chain having one variable and one constant region and the heavy chain having one variable and three to four constant regions (part of which forms the Fc, crystallizable portion). The variable region of the light chain and the heavy chain together forms the antigenbinding site (Fab, antigen binding portion). At the end of each variable region is the hypervariable region (CDR, complementary determining region) and it is this region that allows for numerous conformations for infinite antibody-antigen binding probability.
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治疗性抗体简介
抗体是免疫球蛋白,是体液免疫反应的一部分,由b细胞(浆细胞)分泌。抗体通过与生物体或细胞表面表达的可溶性抗原或配体结合而起作用。在结构上,抗体是由两个重链多肽和两个轻链多肽通过二硫桥连接在一起的y形糖蛋白。轻链和重链由恒定区和可变区组成,轻链有一个可变区和一个恒定区,重链有一个可变区和三到四个恒定区(其中一部分形成Fc,可结晶部分)。轻链和重链的可变区共同形成抗原结合位点(Fab,抗原结合部分)。在每个可变区的末端是高可变区(CDR,互补决定区),正是这个区域允许无限的抗体-抗原结合概率的许多构象。
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