**20. Conclusion**

*Advances in Precision Medicine Oncology*

**19. Antibody-fusion constructs**

involves forming a homogenous product by conjugation at particular sites only. It can be done by altering the structure of antibodies to incorporate non-natural amino acids, which act as a handle for attachment. Available tags have been discovered, such as sortase A tag, which attaches the drug to antibody at the glutamic acid

These are molecules synthesized using recombinant DNA technology. They combine targeting efficiency of IgG and various protein domains. This fusion affects selectivity and PK parameters extensively. Toxic proteins can be used to form immunotoxic compounds such as diphtheria toxin attached to antibodies. Dose-limiting toxicity and immunogenicity are the main challenges in the formation of such complexes. The most successful examples of protein fusion complex are

site and attaches to therapeutic moiety through a polyglycine tag.

**88**

**Figure 3.**

*Types of antibody fragments.*

There is no single magic remedy that acts against all of the diseases. Antibodies are ingenious proteins targeted toward specific foreign molecules inside the body. Their therapeutic use involves their ability to disrupt signal transduction, block receptor, which further affects cell growth and cell death. They also can be used to stimulate the immune system so as to destroy any foreign or ingenious harmful materials. IgG's natural structure can be modified to remove problematic residues and add newly modified proteins for the purpose of targeting and immunostimulating. These attachments come with issues like immunogenicity, acquired resistance. But more research in field of antibody engineering is required to address this issue.
