Abstract
Membrane wetting by biomolecular condensates recently emerged as a critical phenomenon in cell biology. It plays a vital role in a diverse range of processes across different organisms. However, understanding the molecular mechanisms behind this process is still missing. Exploiting ACDAN and LAURDAN properties as nano-environmental sensors in combination with phasor analysis of hyperspectral and lifetime imaging microscopy, we obtained vital information on the process of condensate formation and membrane wetting. The results reveal that glycinin condensates display differences in water dynamics when changing the salinity of the medium as a consequence of rearrangements in the secondary structure of the protein. Remarkably, the analysis of membrane-condensates interaction indicated a correlation between increased wetting affinity and enhanced lipid packing, demonstrated by a decrease in water dipolar relaxation at both protein and polymer systems. These results suggest a general mechanism to tune membrane order by condensate wetting.
Competing Interest Statement
The authors have declared no competing interest.
Footnotes
We have modified the title, extended the discussion, updated the references, and slightly modified figures 1, 2, and 4, for better clarity.