Transient processes continuously proceed in cells: molecule signaling is amplified and diminishes after a certain amount of time, which activates or deactivates cell function including cell division or programmed cell death. During cell division, proteins form stiff, tube-like structures called microtubules to anchor chromosomes and drag them to their envisaged new position. The microtubule’s assemby is a transient process as well and governed by the protein concentration in the cell. The fundamental building blocks of proteins are amino acids. Nature is very efficient in conjugating different amino acids in a sequence-defined way to a macromolecule and to fold it in three dimensions in order to enable the protein’s activity (e.g. in catalysis). The post-doctoral proposal’s overarching aim is to mimic Nature’s transient processes, which could ultimately find application in artificial cells. Here, synthetic precision macromolecules are designed to adopting the protein’s behavior, including the investigation of assembly/disassembly kinetics. As a living cell uses an intrinsic source of energy, the transient self-assembly is triggered by the addition of a fuel. The fuel changes the polarity towards an amphiphilic character, and the chemically activated molecules start to assemble. A reverse reaction revokes the polarity gradient causing the aggregates to disassemble again.