Amphiphilic protein surfactants reduce the interfacial tension of biomolecular condensates.

ABSTRACT: Biomolecular condensates are protein-dense regions in cells that often arise from liquid-liquid phase separation. Interfacial tension is a key determinant of biomolecular condensate behavior, influencing condensate size and interactions with intracellular structures. Certain proteins and RNAs are known to selectively localize to the interface of condensates, where they can regulate condensate function in cells. Previously, we designed amphiphilic proteins that preferentially adsorb to the surface of condensates. These proteins contain one phase-separating domain (RGG) and one non-phase-separating domain (MBP or GST). Here, we demonstrate through direct quantification that these amphiphilic proteins act as surfactants, reducing the interfacial tension of RGG-RGG condensates from ~260 μN/m t

SUBMITTER: Favetta B 

PROVIDER: S-EPMC12262478 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature