Scientists have developed a computational "docking-while-binding" method to de novo design protein homooligomers regulated by small molecules with the corresponding symmetry.1 This method simultaneously optimizes protein-protein and protein-ligand interactions during docking, creating one or more ligand binding sites directly at the protein interface.Previous approaches relied on existing structural information and were limited to heterodimers.[The method allowed the creation of homotrimers, heterodimers, and heterotrimers regulated by amantadine, which they validated in cellular and animal models.1 The protein components have a compact size of approximately 65 amino acids and utilize an FDA-approved orally administered small molecule.[The system is suitable for translational applications in biotechnology and cell therapies.1 The approach extends the chemogenetic toolbox to manipulate biological processes with high temporal precision[1].