Acute hepatopancreatic necrosis disease is an emerging shrimp disease that represents a significant threat to the shrimp farming industry. AHPND is caused by a virulent strain of Vibrio parahaemolyticus (Vp) that harbours the PirAB pore forming toxin. PirAB consists of two components, PirA and PirB, which interact to induce massive mortality in shrimp. The rise of antibiotic resistant Vp from excessive antibiotic use in AHPND management has highlighted the need for alternative methods. Using a de novo AI pipeline called BindCraft, we aimed to inhibit the function of the PirAB toxin by designing proteins specific for PirA. Originally, 96 de novo protein sequences were generated using BindCraft, targeting a conserved hydrophobic pocket within PirA that is predicted to be important for its function. The 96 sequences were filtered to 5 final protein sequences (designated PirA_F611-PirA_F615). Following expression and purification, the binders affinity for PirA was screened using size exclusion chromatography (SEC) and surface plasmon resonance (SPR). We found that PirA_F613 was the only binder with high affinity for PirA and could form a complex. SEC results showed this complex increased in size relative to the individual proteins, and co-eluted as a complex on SDS-PAGE. These results highlight the power of de novo AI pipelines such as BindCraft in designing fast and specific toxin inhibitors. Additionally, de novo proteins such as PirA_F613 may act as future candidates for the control and prevention of AHPND.