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Published on: May 27, 2021
Multi-body fluctuation-induced forces between membrane proteins: Insights from mesoscale simulations
Adrià Bravo Vidal1, Weria Pezeshkian1
1Niels Bohr International Academy, Niels Bohr Institute, University of Copenhagen, Copenhagen, Denmark.
Biophysical Journal
|July 16, 2026
Summary
Membrane proteins organize through indirect interactions, driven by the membrane’s shape fluctuations. Suppressing these fluctuations effectively attracts proteins, influencing cellular processes and nanoparticle design.
Area of Science:
- Biophysics
- Cell Biology
- Computational Biology
Background:
- Protein organization is crucial for cellular functions like signal transduction and adhesion.
- While direct protein binding drives clustering, indirect membrane-mediated forces are also significant.
- Thermal shape fluctuations of membranes can induce protein clustering without direct binding.
Purpose of the Study:
- To investigate the role of fluctuation-induced interactions in the lateral organization of membrane proteins.
- To understand how membrane properties and protein characteristics influence protein clustering.
- To explore the implications for membrane shape remodeling and nanoparticle design.
Main Methods:
- Mesoscale simulations using dynamically triangulated surfaces.
- Parameterization based on local membrane rigidification and curvature induction.
- Analysis across various protein concentrations, membrane tensions, and geometries (planar and spherical).
Main Results:
- Local membrane rigidification by proteins drives non-random organization and segregation above a critical threshold.
- This threshold is sensitive to the degree of rigidification induced by proteins.
- Membrane tension has a minor effect on organization away from the threshold but is significant near it.
- Stiffer proteins nucleate clustering of softer proteins in mixed systems.
- Protein-induced curvature and fluctuation-mediated clustering can remodel membrane shape.
Conclusions:
- Suppression of membrane-shape fluctuations by proteins generates effective attractive forces, driving protein reorganization.
- These findings have broad implications for understanding cellular processes and designing membrane-associated nanoparticles.
- The study provides a comprehensive characterization of fluctuation-induced interactions in membrane protein organization.
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