Main Article Content
In 1986, as the initial monoclonal antibody was accepted by the United States Food and Drug Administration (US FDA), and this time antibody engineering has intensely evolved. Among rapidly emerging therapeutic techniques, antibody engineering based treatment is the best one which is being used to cure human disorders. Antibodies are antigen identifying immunoglobulins which have various repertoire domain capable of antigen specificity. This diverse antibody response is more increased by modifications including somatic recombination, hyper-mutation and post-translational modifications like Fc glycosylation may further upsurge the diversity of effector functions. However, variations in glycan structures effectively helps to the antibody’s functional capabilities. Glycosylation is the modification in protein after the translational process during antibodies synthesis. Glycosylated antibodies play a major role in improving efficiency, pharmacokinetics and safety of curative antibodies. In the pharmacological industries, the regulation and adjustment of therapeutic antibodies is the key point in antibodies engineering. In this review article the recent approaches and novel antibody C-terminals and N-terminals modifications, and their impact on half-life, immunogenicity and effector functions have been discussed. Moreover, the recent progresses in the glycosylation and glycosylation control along with the risk assessments have also been described here.
Keywords: Antibody engineering; Glycosylation; improved efficacy; pharmacokinetics; Therapeutic approaches