The team used high-throughput methods (phage display) to screen many different mutations for increased aggregation resistance. This unbiased approach revealed many surprising findings including, mutations in antibody heavy and light chains are in completely different regions, despite the fact the two chains are structurally very similar.

Both the members of the antibody development lab said that "Collaboration is an essential part of the process. Although our initial work was carried out in the academic environment of the Garvan Institute of Medical Research, we have had significant input from industry collaborators to examine and apply the technology."

Talking about the challenges involved in the production of antibodies, the researchers mentioned that "there are significant failure rates of lead molecules during pre-clinical development due to low stability or aggregation leading to failures in formulation. This places a large burden on pre-clinical development programs. This is further complicated by the move towards high concentration preparations for self-injection, as many antibodies aggregate under such conditions. Formulation changes alone are often not sufficient to overcome the problem. In contrast, we were able to show that a limited number of specific mutations can significantly increase the stability of human antibodies."

The next step for the researchers is to further apply the findings to real-world problems. For this, the researchers are currently working with partners in industry to apply this approach to clinical candidates.