Lipid-protein interaction induced domains: Kinetics and conformational changes in multicomponent vesicles

Area of Science:

• Biophysics
• Cell Biology
• Computational Biology

Background:

• Spatio-temporal organization of proteins and membrane morphology are crucial for cell signaling.
• Previous research explored mechanisms promoting protein aggregation at low concentrations.

Purpose of the Study:

• Investigate how protein affinity for specific lipids affects protein aggregation kinetics.
• Explore lipid-mediated signal amplification and membrane morphological changes.

Main Methods:

• Utilized Monte Carlo simulations to model lipid membranes and proteins.
• Proteins were defined as in-plane fields on a dynamically triangulated surface.

Main Results:

• Strong lipid-protein interactions hasten protein aggregation kinetics, forming large clusters even at low concentrations.
• High protein concentrations led to domain budding, similar to lipid-lipid phase separation.
• Anisotropic proteins with nematic order suppressed domain budding, altering clustering kinetics and conformational changes.

Conclusions:

• Lipid-protein interactions provide a route for lipid-mediated signal amplification.
• Protein clustering and membrane morphology are influenced by protein concentration and their anisotropic properties.