Intrinsically disordered proteins (IDPs) are abundantly present in nature and play important roles in carrying out diverse biological functions, including cellular signaling, cytoplasmic compartment and regulation of gene expression . A class of IDPs, defined as low complexity domains (LCDs), have been recently discovered in association with the dynamic formation of open compartments in cells . These compartments, which are defined as condensates, are formed by liquid-liquid phase separation (LLPS) of proteins and nucleic acids and could underlie important functions and dysfunctions in biology. In addition to their role in biology, these LCDs represent promising building blocks for the design of synthesizing organelles to encode novel biochemical functionalities in bioengineering in a controllable and programmable manner, either alone or conjugated to soluble globular domains .