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An increasing number of proteins with intrinsically disordered domains havebeen shown to phase separate in buffer to form liquid-like phases. Theseprotein condensates serve as simple models for the investigation of the morecomplex membrane-less organelles in cells. To understand the function of suchproteins in cells, the material properties of the condensates they form areimportant. However, these material properties are not well understood. Here, wedevelop a novel method based on optical traps to study the frequency-dependentrheology and the surface tension of PGL-3 condensates as a function of saltconcentration. We find that PGL-3 droplets are predominantly viscous but alsoexhibit elastic properties. As the salt concentration is reduced, their elasticmodulus, viscosity and surface tension increase. Our findings show that saltconcentration has a strong influence on the rheology and dynamics of proteincondensates suggesting an important role of electrostatic interactions fortheir material properties.

Salt-dependent rheology and surface tension of protein condensates using optical traps