Antigen Binding Polypeptides Enhancing TCR/CD3 Affinity and Stability

The patent applies parameter changes by introducing specific amino acid substitutions at defined positions in the heavy and light chains of the antigen binding polypeptide. These substitutions modify the biochemical parameters of the protein structure to enhance both binding affinity and stability simultaneously. The substitutions include positively charged amino acids at specific positions and a tyrosine substitution at position 90, which collectively improve the protein's functional properties.

The patent applies local quality by making targeted modifications at specific locations within the protein structure rather than global changes. The amino acid substitutions are positioned at specific locations in the heavy and light chains where they locally enhance binding interactions and structural stability, while the rest of the protein structure remains intact and functional.

The patent applies parameter changes by modifying the amino acid sequence at specific positions to enhance both binding affinity and effector function. The introduced substitutions create synergistic effects that simultaneously improve recruitment efficiency and the functional output of recruited T cells, addressing both parameters together rather than separately.

The patent applies composite materials by combining multiple amino acid substitutions within the same protein structure to achieve synergistic effects. The combination of positively charged amino acids at different positions and the tyrosine substitution at position 90 creates a composite functional unit that delivers enhanced binding and effector function greater than individual mutations alone.