Onofrio Annunziata: Macromolecular crowding is a property of multicomponent solutions that favors phase separation by excluded-volume interactions between two macromolecules with different size. For protein systems, this phenomenon is important because 1) it affects protein self-assembly in crowded environments such as cell cytoplasm; 2) it is implicated in protein crystallization; 3) it can be used for the rationale design of protein-based materials for enzymology and drug delivery (see above). Polymers are usually added to induce phase separation in protein solutions by macromolecular crowding. However protein-polymer interactions are not well understood and simple excluded-volume models have been only qualitatively successful in describing protein-polymer interactions. Dr. Annunziata’s group experimentally investigate protein-polymer interactions by inducing and characterizing liquid-liquid phase separation (LLPS) in protein-polymer aqueous mixtures. The corresponding phase boundary is represented by a surface in the temperature-concentration phase diagram.
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