This design aims to create an avidity-enhanced binder by fusing two distinct binding proteins, Protein A and Protein B, with a flexible linker. The fusion construct was designed to increase the surface coverage and binding strength to the target. The tertiary structure of the bispecific fusion protein was predicted using AlphaFold3 to assess the correct folding of each domain and the flexibility of the linker. The resulting models were analyzed in Discovery Studio to select designs where both binding domains maintain their native, functional conformations without steric clashes, ensuring the avidity effect is achievable.