English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Thermodynamics of wetting, prewetting and surface phase transitions with surface binding.

MPS-Authors
/cone/persons/resource/persons231550

Bartolucci,  Giacomo
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons40292

Honigmann,  Alf
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/cone/persons/resource/persons145744

Jülicher,  Frank
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Zhao, X. H., Bartolucci, G., Honigmann, A., Jülicher, F., & Weber, C. A. (2021). Thermodynamics of wetting, prewetting and surface phase transitions with surface binding. New Journal of Physics, 23(12): 123003. doi:10.1088/1367-2630/ac320b.


Cite as: https://hdl.handle.net/21.11116/0000-000A-0BC9-8
Abstract
In living cells, protein-rich condensates can wet the cell membrane and surfaces of membrane-bound organelles. Interestingly, many phase-separating proteins also bind to membranes leading to a molecular layer of bound molecules. Here we investigate how binding to membranes affects wetting, prewetting and surface phase transitions. We derive a thermodynamic theory for a three-dimensional bulk in the presence of a two-dimensional, flat membrane. At phase coexistence, we find that membrane binding facilitates complete wetting and thus lowers the wetting angle. Moreover, below the saturation concentration, binding facilitates the formation of a thick layer at the membrane and thereby shifts the prewetting phase transition far below the saturation concentration. The distinction between bound and unbound molecules near the surface leads to a large variety of surface states and complex surface phase diagrams with a rich topology of phase transitions. Our work suggests that surface phase transitions combined with molecular binding represent a versatile mechanism to control the formation of protein-rich domains at intra-cellular surfaces.