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Chair: Sarah Perry "Designing Peptide-Based Complex Coacervates for the Encapsulation of Globular Proteins” Recent work in biological condensates has highlighted the critical role of liquid-liquid phase separation (LLPS) in cellular compartmentalization. Complex coacervates formed from oppositely charged polypeptides serve as excellent model systems to understand these membraneless phenomena. This work investigates the molecular design of peptide-based complex coacervates to understand how sequence, charge density, and hydrophobicity dictate phase behavior and material properties. By utilizing rationally designed poly(lysine)- and poly(glutamate)-based polypeptides, we demonstrate that increasing charge block size and hydrophobicity enhances coacervate stability against salt and increases viscosity. Furthermore, we explore the encapsulation of model proteins, such as hen egg white lysozyme (HEWL), bovine serum albumin (BSA), and various supercharged green fluorescent protein (GFP) variants. These studies reveal that protein uptake is highly dependent on both the specific charge distribution of the protein (e.g., patchy vs. isotropic) and the sequence and hydrophobicity of the coacervating peptides. Additional studies on α-chymotrypsin (ChT) demonstrate that coacervate environments can be precisely tuned to modulate not only protein partitioning but also enzymatic activity. Ultimately, these findings establish quantitative design rules for engineering synthetic membraneless organelles for biocatalysis, protein stabilization, and pharmaceutical applications.
📍 LSL N410