In living systems, fuel-driven assembly is ubiquitous, and examples include the formation of microtubules or actin bundles. These structures have inspired researchers to develop synthetic counterparts, leading to exciting new behaviors in man-made structures. However, most of these examples are serendipitous discoveries because clear design rules do not yet exist. In this work, we show design rules to drive peptide self-assembly regulated by a fuel-driven reaction cycle. We demonstrate that, by altering the ratio of attractive to repulsive interactions between peptides, the behavior can be toggled between no assembly, fuel-driven dissipative self-assembly, and a state in which the system is permanently assembled. These rules can be generalized for other peptide sequences. In addition, our finding is explained in the context of the energy landscapes of self-assembly. We anticipate that our design rules can further aid the field and help the development of autonomous materials with life-like properties.