Session 1C: Inaugural Lectures by Fellows / Associates

Liquid-liquid phase separation is a generic property of proteins and polypeptides.

Abstract: Liquid-liquid phase separation (LLPS) of bio-macromolecules has shown to be associated with membrane-less organelles formation in cells. The cell actively sequesters macromolecules such as proteins and nucleic acids to form liquid condensates for performing various biological functions of the host organism. The phase separation of proteins has also emerged as a crucial nucleation mechanism for protein aggregation associated with various neurodegenerative disorders such as Parkinson’s and Alzheimer’s disease. These protein condensates are dynamic, formed by multivalent interactions, and facilitated by the presence of unstructured and intrinsically disordered domains. We recently showed that LLPS is a generic property of proteins and polypeptides under high crowding or with conditions favoring high intermolecular interactions. We further showed that exposed hydrophobic surface or charge-based interaction, and hydrogen bonding drive the protein/polypeptide LLPS for both single and multicomponent LLPS.