Research on complex coacervates has become instrumental in elucidating key principles of self-assembly within biological condensates. These coacervates emerge through the associative phase separation of oppositely charged polymers, a process primarily dictated by electrostatic interactions and entropy-driven complex formation. Furthermore, complex coacervates represent a highly versatile materials-based platform with diverse biochemical and biomedical applications, such as biosensors, catalysts, and refrigeration-free vaccines. In this study, we design and synthesize sequence-specific peptides as model polymers and utilize a range of model proteins, including a series of supercharged green fluorescent proteins with varying net charges and charge distributions to examine the role of peptide sequence and hydrophobicity on the uptake of protein into our coacervates, as well as the role that the distribution of charges on the protein itself plays. Our ultimate goal is to elucidate design rules whereby the sequence of unstructured peptides can be leveraged to achieve selective uptake of globular proteins of interest.
