Research progress of antibody drugs based on engineering modification of the effector function of the Fc region
XIANG Li
LU Chengyu
Abstract：As biotechnology advances,antibody drugs are crucial in treating diseases.However,wild-type antibodies can't meet the clinical needs for various disease therapies.IgG antibodies,which are prevalent in serum,have a unique Y-shaped structure that enables antigen binding and mediates biological activity,with the Fc(Fragment crystallizable)region playing a key role.Therefore,Fc region engineering has become a vital focus in antibody drug design and development.This article focuses on the Fc region of IgG antibodies and elaborates on its key mechanisms of action in antibody drugs,including the impact of its interactions with Fcγ receptors and Fc neonatal receptor on immune effects and half-life.It details various strategies for Fc region modification,such as amino acid mutations and glycosylation modifications,and discusses the enhancing or reducing effects of these strategies on antibody effector functions and the changes in antibody half-life respectively.By comparing the biological activity functions of different modification types and citing research achievements of Fc modification in antibody drug development,this review looks forward to the possibilities of further exploring Fc region modification in the future and provides inspiration for the research and development of antibody drugs.
Keywords：antibodyFc regionFc engineeringeffector functionhalf-life
Publication Date：2026-02-28
Online Publishing Date：2026-01-28(First online date of this platform, not the publication date of the document)
Pages：10( 109-118 )