<p>Precise helical supramolecular polymers of proteins can only be achieved in vivo by tuning complex, competing supramolecular interactions. This formation suggests a level of cellular control that defines functional structures with high fidelity. Achieving such a phenomenon through synthetic reactions is a challenge owing to the lack of native competing interactions. Here we report that synthetic self-assembled polymers spontaneously disassemble to trigger helical growth of protein units to form well-defined protein tubules in vitro. Cryogenic electron microscopy reconstruction at near-atomic resolution reveals uniform protein helical arrays rather than polymorphic arrays. These uniform arrays are similar to natural microtubules, and the aggregated structure of the sacrificed supramolecular ligands within the protein nanotubule is pentameric. The formation of the protein nanotubules, rather than supramolecular polymer of ligands, regulates the physical properties of the solution and the morphology of liposomes. It was shown that enthalpy–entropy compensation provided by the dissociation of aggregated ligands modulates the homogeneity of the helical pattern of the protein nanotubules, shedding light on the creation of sophisticated bionic materials.</p><p></p>