Building on this platform, we explore the formation and signal-induced structural transition of asymmetric protein assemblies under macromolecularly crowded conditions, which enhance phase separation and spatial organization. In natural systems, sensing events often trigger internal restructuring of membrane-less compartments, such as nucleoli or stress granules. We aim to replicate these post-sensing structural changes within self-assembled fusion protein materials by engineering an aqueous two-phase system (ATPS). We observe morphological rearrangements upon rapamycin addition, indicating that our protein assemblies can reorganize in response to chemical signals—mirroring stimulus-induced remodeling in natural cellular compartments. We employ fluorescence recovery after photobleaching (FRAP) to investigate these dynamics and plan to implement Förster resonance energy transfer (FRET) to assess molecular proximity and interactions. This work provides a tunable platform for studying how sensing and environmental context influence synthetic compartments' behavior.